Search Results

Full Agenda Adhesion GPCR workshop 2024 CINVESTAV, Mexico City, Mexico October 23-25 Download PDF Program HERE < Back to Full Agenda Session VII Physiological and pathological roles of AGPCRs in the nervous system Uncovering the signaling pathway of the ADGRA homolog Remoulade in Drosophila Beatriz Blanco Redondo The Adhesion GPCR Latrophilin Interacts With The Notch Pathway To Control Germ Cell Proliferation Willem Berend Post Uncovering the signaling pathway of the ADGRA homolog Remoulade in Drosophila Beatriz Blanco Redondo Abstract "The Drosophila genome contains five loci encoding adhesion G-protein coupled receptors (aGPCRs). Phylogenetic analysis revealed that the remoulade (remo) gene is a homologue of the vertebrate aGPCR ADGRA family, sharing the same overall receptor domain structure. In vivo expression profiling has shown Remo expression in the central (CNS) and peripheral nervous systems (PNS) of third-instar larvae (L3) and adults. In L3 PNS specimen Remo is expressed in a subset of neurons expressing the DEG/ENaC channel pickpocket (PPK), which is involved in transduction of sensory information like nociception. remoKO larvae and animals, in which remo was knocked down in ppk-neurons through RNA interference, show a higher nocifensive response compared to wildtype remorescue controls indicating that remo is required in PPK-neurons for this behaviour. Furthermore, with the aim to analyse the biochemical properties of Remo, we performed immunoprecipitation analysis. We found that the receptor is cleaved despite the lack of a consensus GPS sequence. Hence, Remo is proteolytically processed, either by the GAIN domain or an alternative protease that cleaved Remo near the GPS. We also aimed at identifying the signaling pathway that Remo is involved in. The mammalian Remo homolog ADGRA2/Gpr124 cooperates with other GPCRs of the Frizzled family, and the transmembrane proteins RECK and Lrp5/6. Collectively these proteins form a cell surface complex that acts as a recognition platform for Wnt ligands. Knowledge of the structural dynamics of this complex is limited and pharmacological and in vivo systems that would allow its characterization are scarce. Remo may serve a role in this peculiar signaling pathway and require further analysis." Authors & Affiliations "Auger, Genevieve Marie1, Bigl, Marina1, America, Michelle2, Vanhollebeke Benoit2, Langenhan Tobias1 1Rudolf Schönheimer Institute of Biochemistry, Division of General Biochemistry, Medical Faculty, Leipzig University, Johannisallee 30, 04103 Leipzig, Germany 2Laboratory of Neurovascular Signaling, Department of Molecular Biology, ULB Neuroscience Institute, Université libre de Bruxelles (ULB), Gosselies B-6041, Belgium" About Beatriz Blanco Redondo "I studied Biomedicine at the University of Barcelona. After my bachelors, I moved to Germany where I obtained my Master’s of Science and PhD degree in Dr. Buchner’s group at the University of Wuerzburg. Shortly after receiving my PhD, I joined Dr. Neil Shneider’s group as a postdoctoral research scientist at Columbia University, New York, where I studied the mechanisms of motor neuron degeneration in Amyotrophic Lateral Sclerosis (ALS). In 2017, I joined the group of Prof. Langenhan where I am studying and characterizing newly generated adhesion GPCR receptors in Drosophila as a model organism for future pharmacological applications." Beatriz Blanco Redondo on the web Blanco-Redondo Lab LinkedIn Google Scholar X (Twitter) The Adhesion GPCR Latrophilin Interacts With The Notch Pathway To Control Germ Cell Proliferation Willem Berend Post Abstract Only available for AGPCR 24 Attendees Authors & Affiliations "Groß Victoria Elisabeth 1, Matúš Daniel 2,3, Kaiser Anette 4, Ließmann Fabian 5, Meiler Jens 5, Schöneberg Torsten 2,6, Prömel Simone 1 1 Institute of Cell Biology, Department of Biology, Heinrich Heine University Düsseldorf, Düsseldorf, Germany 2 Rudolf Schönheimer Institute of Biochemistry, Medical Faculty, Leipzig University, Leipzig, Germany 3 Department of Molecular and Cellular Physiology, Stanford University, Stanford CA, USA 4 Department of Anaesthesiology and Intensive Care, Medical Faculty, Leipzig University, Leipzig, Germany 5 Institute for Drug Discovery, Faculty of Medicine, Leipzig University 6 School of Medicine, University of Global Health Equity, Kigali, Rwanda" About Willem Berend Post "Willem Berend Post is a PhD student in Cell Biology at Heinrich Heine University in Düsseldorf, Germany. His research focuses on the relevance of aGPCRs in physiology and signaling using both in vitro and in vivo approaches." Willem Berend Post on the web Cell Biology LinkedIn < Previous Session Next Session >

Meet the sponsors who make the Adhesion GPCR Workshop 2024 possible, supporting global collaboration and innovation in GPCR research. Home Registration Full Agenda Venue Travel Tips Sponsors Special Issue on Adhesion GPCRs OUR SPONSORS Adhesion GPCR workshop 2024 CINVESTAV, Mexico City, Mexico October 23-25 Sponsor Us Platinum Sponsors Bronze Sponsors Collaborating partners Contact us for sponsorship Register for the Adhesion GPCR 2024 Learn more about the Adhesion GPCR workshop 2024 Up About the event Learn more about the Adhesion GPCR workshop 2024 and its preliminary program. Up About the venue Discover Cinvestav, the host venue for the upcoming workshop. Up Abstract Submission Submit your research abstracts following our guidelines to present at the conference. Up Traveling Tips Find essential tips about Mexico City, including transportation options and local insights.

Full Agenda Adhesion GPCR workshop 2024 CINVESTAV, Mexico City, Mexico October 23-25 Download PDF Program HERE < Back to Full Agenda Session IV AGPCRs signaling in the nervous system BAI1/ADGRB1-mediated Regulation of Mitochondrial Morphology in Axons Joseph Duman Bai1 Is A Novel Neuronal Substrate Of The Psychiatric Risk Kinase TNIK Simeon R. Mihaylov Intricacies Of Complex Assembly And Ligand Interaction In The Adhesion GPCR Latrophilin/Cirl Anne Bormann BAI1/ADGRB1-mediated Regulation of Mitochondrial Morphology in Axons Joseph Duman Abstract Only available for AGPCR 24 Attendees Authors & Affiliations "Tolias, Kimberley F., Departments of Neuroscience and Biochemistry & Molecular Biology, Baylor College of Medicine, Houston, TX 77030" About Joseph Duman "Joseph Duman is an Assistant Professor in the Department of Neuroscience at Baylor College of Medicine, where he studies BAI1's role in the brain and the radiobiology of treatments for brain cancer. He trained at the University of California at Berkeley with John Forte and the University of Washington with Bertil Hille, before joining Kim Tolias' lab at Baylor College of Medicine." Joseph Duman on the web Baylor College of Medicine Kimberley Tolias Lab Bai1 Is A Novel Neuronal Substrate Of The Psychiatric Risk Kinase TNIK Simeon R. Mihaylov Abstract Only available for AGPCR 24 Attendees Authors & Affiliations "Flynn, Helen R.2, Sampedro-Castaneda, Marisol1, Claxton, Suzanne1, Skehel, Mark2, Ultanir, Sila K.1 1Kinases and Brain Development Laboratory, The Francis Crick Institute, UK 2Proteomics Science Technology Platform, The Francis Crick Institute, UK" About Simeon R. Mihaylov " I am a postdoctoral researcher in the kinases and brain development laboratory led by Dr Sila Ultanir at the Francis Crick Institute in London, England. I undertook my BSc in Biochemistry and Genetics at the University of Sheffield followed up by obtaining a PhD in molecular neuroscience at the Sheffield Institute for Translational Neuroscience. I then moved to King's College London, where my interest and passion for kinases in brain health and disease developed. I initially worked on mTOR in the pathogenesis of Tuberous Sclerosis Complex and then moved to the Francis Crick Institute working on the psychiatric risk kinase TNIK. I also work on multiple other kinases in our laboratory implicated in various neurodevelopmental and neurodegenerative disorders. My expertise includes biochemical approaches, proteomics and transcriptomics to name a few. I have recently also developed a strong interest in adhesion GPCRs and in particular, Bai1. " Simeon R. Mihaylov on the web Crick LinkedIn X (Twitter) Google Scholar Intricacies Of Complex Assembly And Ligand Interaction In The Adhesion GPCR Latrophilin/Cirl Anne Bormann Abstract Only available for AGPCR 24 Attendees Authors & Affiliations "Körner, Marek Benjamin; Dahse, Anne-Kristin; Ljaschenko, Dmitrij; Scholz, Nicole (Rudolf Schönheimer Institute of Biochemistry, Division of General Biochemistry, Faculty of Medicine, Leipzig University)" About Anne Bormann "I am a biochemist by training and studied at Leipzig University from 2015 to 2020. During my Bachelor's in 2018, I sought practical lab experience and found a position as a student assistant in Dr. Nicole Scholz's lab. My main topics were protein biochemistry, Drosophila husbandry, and genetics. I was fortunate that Nicole offered me an opportunity to do my Master's and later on a PhD thesis in her group. Since then, I have broadened my horizons with many more techniques in vivo and in vitro, with a main emphasis on the Adhesion GPCR Latrophilin/Cirl. Currently, I am in the final stages of my PhD, and I am looking forward to new projects and ideas." Anne Bormann on the web Rudolf-Schönheimer-Institut für Biochemie Scholz Lab < Previous Session Next Session >

Full Agenda Adhesion GPCR workshop 2024 CINVESTAV, Mexico City, Mexico October 23-25 Download PDF Program HERE < Back to Full Agenda Session II AGPCR signaling pathways and trafficking Localization of putative ligands for adhesion G protein-coupled receptors in mouse tissues. Yuling Feng The ADGRF5/GPR116 receptor is a key regulator of lymphatic endothelial cell identity and function Monserrat Avila Zozaya Adhesion GPCR BAI1/ADGRB1 can block IGF1R-mediated growth signalling, increase radiosensitivity and augment survival in medulloblastoma. Erwin G. Van Meir Site Specific N-Glycosylation Of The N-Terminal Fragment Of ADGRG6 Drives Proteolytic Processing, Trafficking And Signalling Pal Kasturi Localization of putative ligands for adhesion G protein-coupled receptors in mouse tissues. Yuling Feng Abstract Only available for AGPCR 24 Workshop Attendees Authors & Affiliations "Shen,Tingzhen; Bernadyn,Tyler; Kwarcinski, Frank; Gandhi, Riya; Tall, Greg. University of Michigan." About Yuling Feng "I am currently a postdoctoral research fellow working with aGPCR pharmacology and physiology in rodents." Yuling Feng on the web LinkedIn The ADGRF5/GPR116 receptor is a key regulator of lymphatic endothelial cell identity and function Monserrat Avila Zozaya Abstract Only available for AGPCR 24 Workshop Attendees Authors & Affiliations "Serafin D. Stephen, Caron Kathleen M Department of Cell Biology and Physiology at UNC Chapel Hill 111 Mason Farm Road, MBRB, CB 7545. University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA 27599" About Monserrat Avila Zozaya "My doctoral research was focused on investigating the cellular effects of missense lung cancer-mutations in the G-protein-coupled receptor Autoproteolysis-Inducing (GAIN) domain of Latrophilin 3 receptor under the mentorship of Dr. Antony Boucard. I am currently a postdoctoral researcher fellow in Dr. Kathleen Caron's laboratory at UNC. My research focuses on understanding the molecular mechanisms of adhesion GPCRs (aGPCRs) in lymphatic endothelial cells (LECs), a cellular model with unique junction arrangements where aGPCRs are mainly unexplored. " Monserrat Avila Zozaya on the web LinkedIn Caron Lab Antony Boucard Lab Dr. GPCR Adhesion GPCR BAI1/ADGRB1 can block IGF1R-mediated growth signalling, increase radiosensitivity and augment survival in medulloblastoma. Erwin G. Van Meir Abstract Only available for AGPCR 24 Attendees Authors & Affiliations "Yamamoto, Takahiro 1,2*, De Araujo Farias, Virginea 1, Zhu, Dan3; Kuranaga, Yuki1, Parag, Rashed Rezwan 1,4,, Osuka, Satoru1,5 1 Department of Neurosurgery, School of Medicine, University of Alabama at Birmingham, Birmingham, Alabama, USA. 2 Department of Neurosurgery, Kumamoto University, Kumamoto, Japan 3 Department of Neurosurgery, Emory University School of Medicine, Atlanta, Georgia, USA 4 Graduate Biomedical Sciences, University of Alabama at Birmingham (UAB), Birmingham, Alabama, USA 5 O'Neal Comprehensive Cancer Center, University of Alabama at Birmingham (UAB), Birmingham, Alabama, USA " About Erwin G. Van Meir "Dr. Erwin Van Meir is a professor in the UAB Department of Neurosurgery. He was trained in molecular biology at the Universities of Fribourg and Lausanne, Switzerland where he obtained his Ph.D. in 1989. Dr. Van Meir pursued postdoctoral work at the Ludwig Institute for Cancer Research in San Diego and joined the faculty of Emory University in 1998. His research interest lies in understanding the molecular basis for human tumor development and how to use this knowledge to devise new therapeutics that will improve patient survival. Van Meir’s research examines how genetic alterations and hypoxia induce changes in cell biology that promote tumor formation with particular emphasis on adhesion GPCRs ADGRB1 and ADGRB3. Van Meir has developed novel therapeutic approaches for cancer using oncolytic adenoviruses and anti-angiogenic molecules and is currently developing novel small molecule inhibitors of the hypoxia-inducible factor pathway and the epigenetic reader MBD2 (methyl CpG binding protein 2). His research aims to translate these novel agents to testing in clinical trials with the hope to develop novel medicines for cancer treatment." Erwin G. Van Meir on the web Google Scholar Site Specific N-Glycosylation Of The N-Terminal Fragment Of ADGRG6 Drives Proteolytic Processing, Trafficking And Signalling Pal Kasturi Abstract "ADGRG6 is a member of the adhesion G-protein-coupled receptor (aGPCR) family, known to play a role in myelination, placentation, blood vessel, and inner ear development. Like many other aGPCRs, ADGRG6 undergoes autoproteolysis at the GPCR-autoproteolysis site (GPS) enclosed within the larger GAIN domain to generate the N-terminal (NTF) and C-terminal fragments (CTF). These cleaved fragments join to form the heteromeric ADGRG6 receptor complex. ADGRG6 NTF has multiple extracellular domains like CUB, PTX, SEA, hormone binding domain, and the GAIN domain, which regulate G-protein signaling by binding to extracellular matrix proteins and mechanotransduction. The short stachel sequence at the extreme N-terminal end of the CTF functions as a tethered agonist to activate cAMP signaling. GPCR signaling and trafficking can be regulated by several different post-translational modifications (PTM). Stehlik et al. have reported that ADGRG6 expressed in lipopolysaccharide stimulated human umbilical vein endothelial cells is N-glycosylated. However, it is unclear which domains of ADGRG6 are N-glycosylated and how this might affect the overall molecular pharmacology of the receptor. Furthermore, are there spatial roles of N-glycosylation in ADGRG6 processing, trafficking, signalling and in-vivo functions? To address these gaps in knowledge, we used biochemical and cell-biological approaches using cell-lines overexpressing wild-type and N-glycosylation mutants of ADGRG6. We observed that N-glycosylation specifically takes place in the NTF and not the CTF of ADGRG6. Our results demonstrate that specific N-glycan residues in different domains of the extracellular NTF of ADGRG6 have distinct roles in ADGRG6 autoproteolysis, furin cleavage, membrane trafficking, and G-protein signalling. In the future, we plan to decipher the roles of N-glycosylation of ADGRG6 in organogenesis and tissue development using zebrafish models." Authors & Affiliations "Anandhu Jayaraman: Department of Biology, Ashoka University Prabakaran Annadurai: Department of Biology, Ashoka University. Currently: University of Leipzig Mansi Tiwari: Department of Biology, Ashoka University. Currently: University of Aberdeen Priyadatha Sajan: Department of Biology, Ashoka University, Currently: University of Groningen Nayonika Chatterjee: Department of Biology, Ashoka University Prateek Sibal: Department of Biology, Ashoka University" About Pal Kasturi "I received my bachelor’s degree in Physiology from Presidency College, University of Calcutta and went on to complete my masters from Madurai Kamaraj University. During my PhD training, I worked in the laboratory of Dr. Kathryn Defea at the University of California, Riverside. For my PhD thesis, I worked on non-canonical, scaffold driven signaling by protease activated receptor-2 (PAR2). I joined University of Texas Southwestern Medical Center, for my postdoctoral training. Here, I worked on the regulation of the Sonic Hedgehog pathway by GPCRs which localized to the primary cilia. I then joined the laboratory of Dr. Velia Fowler, at the Scripps Research Institute, as a Judith Graham Poole postdoctoral fellow to work on the role of cytoskeletal proteins in megakaryocyte to platelet differentiation. I joined the Department of Biology at Ashoka University in 2020 as an assistant professor." Pal Kasturi on the web Ashoka University < Previous Session Next Session >

Full Agenda Adhesion GPCR workshop 2024 CINVESTAV, Mexico City, Mexico October 23-25 Download PDF Program HERE < Back to Full Agenda Welcoming Remarks < Previous Session Next Session >

Full Agenda Adhesion GPCR workshop 2024 CINVESTAV, Mexico City, Mexico October 23-25 Download PDF Program HERE < Back to Full Agenda Plenary Lecture Identification and Functional Characterization of Adhesion GPCRs As Steroid Hormone Receptors and Hearing and Balance Receptors Abstract Only Available for AGPCR24 Attendees About Jin-Peng Sun "Since starting my laboratory in 2011, I has focused on G protein coupled receptors, in particular, the ligand identification, physiological functions and molecular mechanism of biased signaling of GPCRs. Our first main research aspect is the identification of endogenous ligand of GPCRs. We have identified the receptor subfamily to sense the steroid hormones. For instance, membrane receptor GPR97 is able to sense glucocorticoid to mediate its rapid actions, the progesterone and 17-hydroxyprogesterone membrane receptor are GPR126. We also identified DHEA, DHEAS and DOC are endogenous ligands of GPR64 etc (Nature, 2021a, Nat Chem Biol 2022, PNAS 2022b). Our second main research aspect is dissecting the molecular mechanism underlying sensation of force, ordor, itch and taste by GPCRs. We have elucidated the mechanism of receptors' perception of itch, olfactory and force (Nature 2021b, 2022a, 2022b, 2023a, 2024). Our third main research aspect is working mechanism of GPCR. For arrestin mediated biased signaling, we have proposed the “flute model” and “poly proline region docking theory” etc. to explain the arrestin mediated GPCR functions (Nature communications, 2015, 2021, 2022; PNAS 2021, Molecular Pharmacology, 2017; Recommended by Faculty 1000, Nature Chemical Biology 2018). We identified that arrestin can mediated AT1R/TRPC3 or M3R/TRPC3 coupling by forming a complex of AT1R/β-arrestin-1/PLCγ/TRPC3 or M3R//β-arrestin-1/TRPC3 (Nature communications, 2017, Nature communications, 2018). We also identified that orphan receptor GPR64 forms complex with β-arrestin-1 and CFTR at apical membrane of efferent ductulus to regulate the salt/water metabolism (eLife 2018, Faculty 1000 recommendation). Our fourth main research aspect is ligand coding mechanisms and structural aided drug discovery of GPCR. We have decoded the mechanisms underlying recognition of fish oil (unsaturated fatty acids) and other lipids by GPCRs (Science 2023, Science Advance 2021, PNAS 2023, Nature Metabolism 2023), recognition of amine containing hormones by GPCRs (Cell 2021, 2023, Nature 2023b), bile acids or its derivatives by GPCRs (Nature 2020)." Jin-Peng Sun on the web Google Scholar LinkedIn < Previous Session Next Session >

Full Agenda Adhesion GPCR workshop 2024 CINVESTAV, Mexico City, Mexico October 23-25 Download PDF Program HERE < Back to Full Agenda Session VI AGPCRs shaping the nervous system ADGRCs in glutamatergic synapse formation, maintenance and degeneration Yimin Zou Antibody-drug conjugates targeting CD97 in glioblastoma Dimitris Placantonakis Adhesion G protein-coupled receptor latrophilin-3 (ADGRL3) modulation of dopaminergic neurotransmission Nicole Perry-Hauser ADGRCs in glutamatergic synapse formation, maintenance and degeneration Yimin Zou Abstract "ADGRCs (Celsr1-3) are components of the conserved planar cell polarity (PCP) pathway, which establishes and maintains cell and tissue polarity along the tissue plane in all tissues. Work from our lab showed that the PCP components, including ADGRC2 and ADGRC3, are localized in the developing and adult synapses and interact with synaptic scaffold proteins and glutamate receptors and are responsible for the formation and stability of the vast majority of glutamatergic synapses in the mammalian brain. Initial impairment of synaptic functions, which occurs early in Alzheimer’s disease, and subsequent massive loss of synapses are closely correlated with the decline of cognitive function. We showed that oligomeric Aβ binds to ADGRC3 on the same domain required for the interaction with Frizzled3, weakens their interaction and assists Vangl2 in disassembling synapses. Conditionally knocking out Ryk, required for Vangl2 function, protected synapses and preserved cognitive function in a mouse model for Alzheimer’s. Massive synapse loss in the prefrontal cortex is a hallmark of massive depressive disorder. Injection of low-dose ketamine, an antidepressant, can lead to acute (in several hours) and sustained (up to several weeks) antidepressive effects. Restoration of synaptic connections induced by low-dose ketamine has been found associated with the sustained antidepressive effects. We showed that ADGRC2 and ADGRC3 are required for the restoration of glutamatergic synapses in prefrontal cortical neurons of chronically stressed animals and their behavioral remission induced by low-dose ketamine. I will also present ongoing work on the signaling mechanisms of how ADGRCs regulate synapse formation, maintenance and plasticity." About Yimin Zou "I received Ph.D from University of California at Davis and San Diego in 1995 and then postdoctoral training from University of California, San Francisco in 2000. I was an assistant and then associate professor with tenure at the University of Chicago from 2000 to 2006 and moved to University of California San Diego as an Associate Professor in 2006. I became full professor in 2011 and Vice Chair of the Neurobiology Department at UC San Diego in 2012. I served as the Chair of the Neurobiology Department at UC San Diego from 2014 to 2017. My research focus is the mechanisms of neural circuit development, function and disease." Yimin Zou on the web UC San Diego Antibody-drug conjugates targeting CD97 in glioblastoma Dimitris Placantonakis Abstract "Glioblastoma (GBM) is the most common and aggressive primary brain malignancy. Several adhesion G protein-coupled receptors (aGPCRs) have recently been shown to play critical roles in GBM biology. We showed that CD97 (ADGRE5), in particular, drives tumor growth via effects on GBM stem cell self-renewal and metabolism, but also has a therapeutically favorable expression pattern: it is highly expressed in all GBM specimens, but is absent from healthy brain tissue. To exploit this expression profile, we have developed antibody-drug conjugates (ADCs) targeting CD97, by screening a synthetic human antibody library. We initially tested the ADC using in vitro WST-8 viability assays in human GBM cell lines and cell types that lack CD97. We observed significantly lower LD50 values in patient-derived and U87 GBM cell cultures vs. CD97-lacking cells. We also found significantly lower LD50 values when treating human GBM cells with the ADC (0.6788 nM), as compared to control ADC targeting RSV glycoprotein F (19.964 nM). In vivo intratumoral administration of the ADC in patient-derived GBM xenografts in the brain of immunodeficient mice resulted in significant reduction of tumor growth and prolongation of survival of host mice. Collectively, these data suggest that ADCs targeting CD97 impair tumor growth in preclinical GBM models and are promising candidates for future clinical trials." Authors & Affiliations "Groff, Karenna; Donaldson, Hayley; Anderson, Sebastian; Pitti, Kiran; Wang, Shuai; Park, Christopher; Hattori, Takamitsu; Koide, Shohei; Placantonakis, Dimitris New York University Grossman School of Medicine" About Dimitris Placantonakis "Dimitris Placantonakis is a neurosurgeon-scientist at NYU Grossman School of Medicine in New York. As a clinician, he specializes in surgical treatment of brain tumors. His laboratory studies oncogenesis in glioblastoma, the most common brain malignancy, and chromatin organization in human neural development. His group has been particularly interested in the role adhesion GPCRs play in glioblastoma biology and their therapeutic targeting." Dimitris Placantonakis on the web Placantonakis Lab Google Scholar LinkedIn Adhesion G protein-coupled receptor latrophilin-3 (ADGRL3) modulation of dopaminergic neurotransmission Nicole Perry-Hauser Abstract Only available for AGPCR 24 Attendees Authors & Affiliations "Nicole A. Perry-Hauser1,2, Arturo Torres Herraez1,2, Dan Lowes1,2, Ying Zhu1,2, Siham Boumhaouad1,3, Eugene V. Mosharov1,2,4, David Sulzer1,2,4, Christoph Kellendonk1,2, and Jonathan A. Javitch1,2 1Departments of Psychiatry and Molecular Pharmacology and Therapeutics, Columbia University, New York, NY 10032; 2Division of Molecular Therapeutics, New York State Psychiatric Institute, New York, NY 10032; 3 Physiology and Physiopathology, Faculty of Sciences, Mohammed V University, Rabat 1014, Morocco; 4Department of Neurology, Columbia University, New York, NY 10032" About Nicole Perry-Hauser "I am an associate research scientist endeavoring to build a productive, independent scientific research career in adhesion G protein-coupled receptor (aGPCR) biology. My long-term research interests involve resolving signaling pathways downstream of aGPCRs and establishing how/if these receptors’ adhesive properties influence signaling events, and in turn whether signaling impacts synapse formation and neuronal wiring. I initially became interested in GPCR signal transduction during my graduate training in the Department of Pharmacology at Vanderbilt University where I studied under the co-mentorship of Dr. Vsevolod V. Gurevich and Dr. Tina M. Iverson. I then pursued a postdoctoral research position under the mentorship of Dr. Jonathan A. Javitch in the Department of Psychiatry at Columbia University Irving Medical Center." Nicole Perry-Hauser on the web LinkedIn Research Gate Pubmed Dr. GPCR < Previous Session Next Session >

Full Agenda Adhesion GPCR workshop 2024 CINVESTAV, Mexico City, Mexico October 23-25 Download PDF Program HERE < Back to Full Agenda Session III Molecular tools and biosensors directed at AGPCR signaling and function The NTF Release Sensor Approach for Drug Discovery for Human Adhesion GPCRs Stephanie Häfner bioSens-All: A Multiparametric BRET-Based Platform for Comprehensive Profiling of adhesion GPCR Signaling and Pharmacology-Enabling Drug Discovery Laurent Sabbagh Characterizing hADGRE5/CD97 Activation and Signaling: A Mechanical Stimulation BRET-Based Approach (MS-BRET) Ana Lilia Moreno Salinas The NTF Release Sensor Approach for Drug Discovery for Human Adhesion GPCRs Stephanie Häfner Abstract "G Protein-coupled receptors (GPCRs) are common drug targets, yet no approved drugs exist for the Adhesion G Protein-coupled receptors (aGPCRs or ADGRs). This gap is due to their unique autoproteolytic cleavage in the GAIN domain, creating a heterodimer of an N-terminal fragment (NTF) and a C-terminal fragment (CTF), posing challenges for traditional drug discovery. To address this, we developed the NTF release sensor (NRS), a genetically encoded reporter that facilitates visualization and quantification of aGPCR NTF-CTF separation events both in vitro and in vivo. The NRS fuses the extracellular region of any given aGPCR with a cleavage module from a Notch receptor. Upon NTF dissociation, an intracellular transcription factor (reporter module) is released, generating a specific, measurable biochemical signal. The NRS system has recently been validated in vivo by targeting the latrophilin-type aGPCR Cirl/ADGRL in Drosophila, revealing NTF release and receptor dissociation within the developing nervous system. It was then adapted for the human aGPCRs CD97/ADGRE5 and Latrophilin/ADGRL3 and tested in HEK293T cells using a luciferase assay to detect NTF release events. After validating the functionality of the NRS and demonstrating its utility for monitoring aGPCR dissociation across different species, we plan to adapt this technology for high-throughput screening of pharmacological compound libraries to identify potential therapeutic substances for aGPCRs. By leveraging self-cleavage and NTF release, the NRS technology offers a novel approach distinct from conventional GPCR drug discovery methods. This tailored system aims to expedite the identification of drugs targeting the unique aGPCR receptor family and customize the method for disease-relevant human aGPCRs." Authors & Affiliations "Dahse, Anne-Kristin; Annadurai, Prabakaran; Demirbaş, Berkay; Kemkemer, Marguerite; Langenhan, Tobias; Scholz, Nicole Rudolf Schönheimer Institute of Biochemistry, Divison of General Biochemistry, Medical Faculty, Leipzig University, Leipzig, Germany" About Stephanie Häfner "I am a trained chemist with extensive biochemical experience. After earning my Master of Science in Chemistry, I pursued my PhD in Dr. Michael Schaefer’s group at Leipzig University, Germany, focusing on drug screening and utilizing electrophysiological and imaging techniques to study TRP ion channels. Immediately following my PhD, I joined Dr. Guillaume Sandoz's group in 2019 as a postdoctoral research scientist at Université Côte d‘Azur, France. There, I investigated Two-Pore-Potassium channels using electrophysiology, molecular and chemical biology techniques, and fluorescence imaging. In 2021, I joined Dr. Tobias Langenhan's group, where I currently manage a project to establish a drug screening assay for Adhesion GPCRs using a specialized sensor system and mentor PhD students." Stephanie Häfner on the web LinkedIn Scholz Lab Langenhan Lab bioSens-All: A Multiparametric BRET-Based Platform for Comprehensive Profiling of adhesion GPCR Signaling and Pharmacology-Enabling Drug Discovery Laurent Sabbagh Abstract "The 3rd generation bioSens-All platform combines BRET-based biosensors that are highly adaptable to the needs of discovery projects for small molecules, peptides, and antibodies. The platform has been successfully used internally to identify biased small molecule negative allosteric modulators for protease-activated receptor 2 (PAR2). The platform revealed different mechanisms-of-action of our lead compound when benchmarked against other antagonists of PAR2. In addition, the platform was used to develop assays for high-throughput screening for challenging adhesion GPCRs. These examples will demonstrate how the bioSens-All platform was used to advance projects from discovery to preclinical candidate nomination and to provide the tools to advance adhesion GPCR biology." Authors & Affiliations "Ana Lilia Moreno Salinas (2), Arturo Mancini (1), Raida Jallouli (2), Richard Leduc (2) (1)Domain Therapeutics North America Inc, Montréal, Québec, Canada (2) Department of Pharmacology-Physiology, Université de Sherbrooke, Québec, Canada" About Laurent Sabbagh "Laurent holds a Ph.D. in immunology from McGill University. Following his doctoral degree Dr. Sabbagh undertook post-doctoral fellowships at the Ontario Cancer Institute and the University of Toronto before being recruited by University of Montreal as an assistant professor working on the role of TNF receptors in immunological memory, inflammation and hematological malignancies. In the fall of 2013, Dr. Sabbagh was recruited by Vertex Pharmaceuticals (Canada) where he worked on biomarker discovery for inflammatory bowel disease and small molecules drug discovery for polycystic kidney disease. Subsequently, Dr. Sabbagh led research projects aimed on drug discovery of small molecules for the treatment of inflammatory disorders and cancer at Paraza Pharma Inc. in Montreal. Laurent is currently leading DTNA discovery group working on GPCRs in immuno-oncology to discover new molecules and antibodies." Laurent Sabbagh on the web Domain Therapeutics Characterizing hADGRE5/CD97 Activation and Signaling: A Mechanical Stimulation BRET-Based Approach (MS-BRET) Ana Lilia Moreno Salinas Abstract Only available for AGPCR 24 Attendees Authors & Affiliations "Arturo Mancini (2), Samya Aouad (2,3), Herthana Kandasamy (2), Sandra Morrissette (2), Arhamatoulaye Maiga (4), Michel Bouvier (4), Richard Leduc (1), Laurent Sabbagh (2) 1. Department of Pharmacology-Physiology, Université de Sherbrooke, Sherbrooke, Quebec, Canada 2. Domain Therapeutics North America Inc., Montreal, Quebec, Canada 3. Université Claude Bernard - Lyon, Faculté de Pharmacie, Lyon, France 4. Department of Biochemistry and Molecular Medicine, Institute for Research in Immunology and Cancer (IRIC), Université de Montréal, Montreal, Quebec, Canada " About Ana Lilia Moreno Salinas "I am currently part of a dynamic research team dedicated to advancing the understanding of G protein-coupled receptors (GPCRs), with a particular focus on the adhesion GPCRs (aGPCRs) family. My expertise lies in exploring the biological properties and signaling pathways activated by aGPCRs, investigating their roles in both normal physiological and pathological conditions. Our research aims to leverage this knowledge to identify novel pharmacological targets and contribute to the development of innovative treatments for a range of diseases, including psychiatric disorders and cancer." Ana Lilia Moreno Salinas on the web ResearchGate LinkedIn < Previous Session Next Session >

Full Agenda Adhesion GPCR workshop 2024 CINVESTAV, Mexico City, Mexico October 23-25 Download PDF Program HERE < Back to Full Agenda Session I Tethered agonist - dependent/independent activation mechanism in AGPCRs Signaling Properties of ADGRL3 Signe Mathiasen An ECR-Mediated and TA-independent Mechanism of aGPCR Activation: Direct Communication of Extracellular Region with Transmembrane Domain in a Holo-Adhesion GPCR Demet Araç Heterogeneity of Tethered Agonist Signaling in Adhesion G Protein-Coupled Receptors Andrew Dates Discriminating between the extracellular scaffolding and G protein signaling roles of GPR56/ADGRG1 via the characterization of a non-cleavable point mutant knock-in mouse, H381S Frank Kwarcinski Tethered Peptide Activation Mechanism of Adhesion GPCRs Peng Xiao Signaling Properties of ADGRL3 Signe Mathiasen Abstract Only available for AGPCR 24 Workshop Attendees Authors & Affiliations "Rosell, Júlia (1) Holmkvist, Jesper L. (1) Arastoo, Mohammad Reza (1) Vejre, Phillip C. (1) Regmi, Rajesh (1) Perry-Hauser, Nicole A. (2) Bendix, Poul Martin (3) Javitch, Jonathan A. (2) Mathiasen, Signe (1) 1. Department of Biomedical Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark. 2. Departments of Psychiatry and Molecular Pharmacology and Therapeutics, Columbia University Vagelos College of Physicians and Surgeons, New York, New York, USA; Division of Molecular Therapeutics, New York State Psychiatric Institute, New York, New York, USA 3. Niels Bohr Institute, Faculty of Natural Sciences, University of Copenhagen, Copenhagen, Denmark" About Signe Mathiasen "2022-present Assistant Professor (Tenure Track) and Group Leader Department of Biomedical Sciences, University of Copenhagen. 2020 – 2022: Assistant Professor Department of Biomedical Sciences, University of Copenhagen. 2014-2021: Postdoc / Assistant Professor Department of Psychiatry, Columbia University, New York, USA. New York State Psychiatric Institute, Research Foundation for Mental Hygiene, New York, USA. Postdoc Supervisor Professor Jonathan Javitch 2013: PhD in Nanoscience/Biophysics. Department of Chemistry, University of Copenhagen, Copenhagen Denmark. PhD Supervisor Professor Dimitrios Stamou." Signe Mathiasen on the web University of Copenhagen Mathiasen Group An ECR-Mediated and TA-independent Mechanism of aGPCR Activation: Direct Communication of Extracellular Region with Transmembrane Domain in a Holo-Adhesion GPCR Demet Araç Abstract "According to the Tethered Agonist (TA)-mediated model of aGPCR activation, the ECR acts as a protective cap for the TA peptide to hide it within the GAIN domain. However, several recent observations suggest that other mechanisms of aGPCR activation are possible. For example, some aGPCRs do not undergo autoproteolysis, which is required for TA release. Even the aGPCRs that are cleaved do not always require cleavage for mediating some aspects of wild type functions. It has been suggested that the TA can regulate receptor signaling without coming out of the GAIN domain or by being partially exposed, however the recent TA-bound 7TM structures of multiple aGPCRs showed that the critical phenylalanine residue and other important TA residues have to reach deep into the 7TM orthosteric pocket for receptor activation, suggesting that non-release or partial release of the TA is unlikely to activate the receptor. In this talk, I summarize accumulating data from our lab and the aGPCR field that suggests an additional model in which the conformation of the Extracellular Region (ECR) has a direct role in modulating the 7TM signaling, independently of TA-mediated activation. Our results provide evidence for the ECR-mediated activation of aGPCR as a complementary mechanism for the TA-mediated activation of aGPCRs. Many biological forces are smaller than 200 pN, the force that is needed to separate the TA from the GAIN domain. To sense these smaller forces, and to regulate aGPCR function on and off, a mechanism that does not depend on ECR dissociation and TA exposure might be at work. At low force or no force conditions, aGPCR may be reversibly regulated by binding and dissociation of a ligand to the ECR without ECR shedding and TA exposure. In this ECR-mediated mechanism of activation, the ECR-7TM communication is altered by transient interactions between ECR and 7TM. The TA peptide remains at its original position and is not involved in signaling. Because the TA-mediated mechanism is a “one and done” mechanism that is irreversible and prevents the receptor from going back to its inactive resting state, the ECR-mediated mechanism may operate in situations where a reversible regulation is needed. The ECR-mediated mechanism may also enable responding to compressing forces on the receptor, that directly “push” on the protein. In cases where a large “pulling” force is executed on the ECR, the ECR may be removed from the 7TM releasing the tethered agonist and activating the aGPCR irreversibly but acutely. ECR-mediated mechanism opens new possibilities for drugging aGPCRs. Future work that dissects different activation mechanisms of aGPCRs in different physiological contexts will shed light on this fascinating family of receptors. " Authors & Affiliations "Kordon Szymon P.1, 2, Cechova Kristina3, Bandekar Sumit J.1, 2, Ethan Dintzner1, 2, Leon Katherine1, 2, Dutka Przemysław1, Siffer Gracie3, Kossiakoff Anthony A.1, Sando Richard 4, Vafabakhsh Reza3, Araç Demet1, 2 1. Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago; 2. Neuroscience Institute, Institute for Biophysical Dynamics, and Center for Mechanical Excitability, The University of Chicago, 3. Department of Molecular Biosciences, Northwestern University; 4. Vanderbilt University" About Demet Araç "Demet was an undergraduate at Bilkent University in Turkey, where she majored in Molecular Biology and Genetics. She moved to the University of Texas Southwestern Medical Center at Dallas in 2000 to work with Dr. Jose Rizo-Rey as a graduate student to elucidate the mechanisms of neurotransmitter release. After finishing her graduate training, she joined Dr. Axel Brunger’s lab at Stanford University to study the structure and function of cell-adhesion proteins at the synapse. In 2013, Demet began her independent research career at the University of Chicago within the Department of Biochemistry and Molecular Biology." Demet Araç on the web Araç Laboratory at UChicago X (Twitter) Heterogeneity of Tethered Agonist Signaling in Adhesion G Protein-Coupled Receptors Andrew Dates Abstract Only available for AGPCR 24 Workshop Attendees Authors & Affiliations "Daniel T.D. Jones (Harvard Medical School); Jeffrey S. Smith (Harvard Medical School, Brigham and Women's Hospital); Meredith A. Skiba (Harvard Medical School); Maria F. Rich (University of Cincinnati School of Medicine); Maggie M. Burruss (Harvard Medical School); Andrew Kruse (Harvard Medical School); Stephen C. Blacklow (Harvard Medical School)" About Andrew Dates "Drew Dates received his B.S. in Biological Chemistry from Carnegie Mellon University in 2018. As an undergraduate, he studied opioid receptor trafficking and G protein conformational dynamics in the laboratories of Manojkumar Puthenveedu and Roger Sunahara, respectively. As part of his doctoral work in the Blacklow laboratory at Harvard Medical School, Drew studied structure-function relationships in the Adhesion Family of GPCRs." Andrew Dates on the web Harvard Medical School Discriminating between the extracellular scaffolding and G protein signaling roles of GPR56/ADGRG1 via the characterization of a non-cleavable point mutant knock-in mouse, H381S Frank Kwarcinski Abstract Only available for AGPCR 24 Workshop Attendees Authors & Affiliations ""Tyler F. Bernadyn, Mariane Nascimento, Xinyi Lu, Pauline L. Pan, Michael Holinstat and Gregory G. Tall Department of Pharmacology, University of Michigan "" About Frank Kwarcinski "I am research faculty within the department of Pharmacology at the University of Michigan. I work under the supervision of Dr. Gregory Tall and our research primarily focuses on the structural and biochemical characterization of adhesion GPCRs (AGPCR) for mechanism of action and pathogenesis studies. We utilize several genetically modified mouse models to investigate requirements for receptor activator and continuously work to identify novel chemical modulators of AGPCRs through assay development and high-throughput screening efforts. I have previous work experience at two separate contract research organizations centered on assay development, and I am formally trained as a chemical biologist." Frank Kwarcinski on the web LinkedIn Tethered Peptide Activation Mechanism of Adhesion GPCRs Peng Xiao Abstract Only available for AGPCR 24 Workshop Attendees About Peng Xiao "I joined Prof. Jin-Peng Sun’s Lab since I graduated from Shandong University in 2012, and worked under the guidance of Prof. Sun as a postdoc/research associate/assistant professor. Since then, I have been working on dissecting the three-dimensional architecture and underlying molecular signaling mechanism of GPCR using cryo-electron microscopy (cryo-EM). So far, I have published 20 peer-reviewed papers as correspondence (or co- correspondence) or first (or co-first) authors, among which, four papers were published in Nature (2022a, 2022b, 2021, 2020); one paper was published in Cell (2021); on paper was published in Science (2023); two papers were published in Nat Chem Biol. (2022, 2018)." Peng Xiao on the web ResearchGate < Previous Session Next Session >

Full Agenda Adhesion GPCR workshop 2024 CINVESTAV, Mexico City, Mexico October 23-25 Download PDF Program HERE < Back to Full Agenda Session V Structural mechanisms of AGPCR signaling and function Structural Determinants Of GAIN Domain Autoproteolysis And Cleavage Resistance Of Adhesion G Protein-Coupled Receptors Fabian Pohl Structural studies of the CELSR1 extracellular region reveal a compact multidomain module of fourteen domains which regulates signaling Sumit Bandekar Unveiling the GPS Cleavage Mechanism in ADGRL1 with QM/MM Florian Seufert Structural Determinants Of GAIN Domain Autoproteolysis And Cleavage Resistance Of Adhesion G Protein-Coupled Receptors Fabian Pohl Abstract "The GPCR autoproteolysis-inducing (GAIN) domain is a hallmark feature of adhe-sion G-protein coupled receptors (ADGRs), as this extracellular domain contains an integral agonistic sequence (Stachel) for activation via binding to the 7-transmembrane (7TM) helical domain of the receptor. Many ADGRs are autoproteo-lytically cleaved at the GPCR proteolysis site (GPS), an HXS/T motif within the GAIN domain. However, several ADGRs can be activated without GPS cleavage. We de-termined the crystal structure of the human ADGRB2/BAI2 hormone receptor (HormR) and GAIN domains and found that this ADGR is resistant to autoproteolysis despite the presence of a canonical HLS sequence at the GPS. By structural com-parison and with the help of molecular dynamics (MD) simulations we identified several unique structural features that are important for autoproteolytic cleavage, beyond the canonical HXS/T motif. Disruption of these features reduced autoproteo-lytic activity in ADGRL1/LPHN1 and restored cleavage competence of AD-GRB3/BAI3. Furthermore, conservation analysis indicates that wild type ADGRB2 and ADGRB3 are GPS cleavage-incompetent receptors." Authors & Affiliations "Fabian Pohl1, Florian Seufert2, Yin Kwan Chung3, Daniela Volke1, Ralf Hoffmann1, Torsten Schöneberg4, Tobias Langenhan3, Peter W. Hildebrand2, Norbert Sträter1 1 Institute of Bioanalytical Chemistry, Leipzig University, Deutscher Platz 5, 04103 Leipzig, Germany 2 Institute of Medical Physics and Biophysics, Leipzig University, Härtelstr. 16-18, D-04107 Leipzig 3 Rudolf-Schönheimer-Institute of Biochemistry, Division of General Biochemistry, Leipzig University, Johannisallee 30, D-04103 Leipzig 4 Rudolf-Schönheimer-Institute of Biochemistry, Division of Molecular Biochemis-try, Leipzig University, Johannisallee 30, D-04103 Leipzig" About Fabian Pohl "Mar 2023 – Today Postdoc, University Leipzig, Group of Prof. Langenhan Apr 2016 – Nov 2022 PhD candidate, University Leipzig, Group of Prof. Sträter Oct 2011 – Mar 2016 Master of Science in chemistry, University Leipzig Oct 2008 – Sep 2011 Bachelor of Science in chemistry, University Leipzig" Fabian Pohl on the web Langenhan Lab Structural studies of the CELSR1 extracellular region reveal a compact multidomain module of fourteen domains which regulates signaling Sumit Bandekar Abstract "Cadherin EGF Laminin G seven-pass G-type receptors (CELSRs) are conserved adhesion G protein-coupled receptors; they are essential for embryogenesis and neural development. CELSRs have large and enigmatic extracellular regions (ECRs) with nine cadherin repeats and a variety of adhesion domains which couple cell adhesion to signaling. CELSRs regulate planar cell polarity, including the closure of the neural tube. Despite numerous cell and animal studies, molecular details on CELSR proteins are sparsely available, precluding an integrative understanding of CELSR biology. Here, we report the 3.8 Å cryo-EM reconstruction of the CELSR1 ECR which enables unambiguous assignment of the 14 domains within the structure. These domains form a compact module mediated by robust and evolutionarily conserved interdomain interactions. This compact module provides a plethora of potential ligand binding sites for the various adhesion domains within the structure and hints at a model where the compact module could be pulled apart by robust mechanical force. We present biophysical evidence that the CELSR1 ECR forms an extended dimer in the presence of Ca2+, which we propose represents the cadherin repeats dimerizing in a configuration similar to protocadherins. We employ cellular assays with full-length CELSR1 and truncation constructs to assess the adhesive and signaling functions of this protein. We assign the N-terminal CADH1-8 module as necessary for cell adhesion and we show the C-terminal CAHD9-GAIN module regulates signaling. Our work provides molecular context to the literature on CELSR function and lays the groundwork for further elucidation of structure/function relationships." Authors & Affiliations "Garbett, Krassimira, Kordon, Szymon P., Shearer, Tanner, Sando, Richard C.*, and Araç, Demet* Department of Biochemistry and Molecular Biology, The University of Chicago Neuroscience Institute, Institute for Biophysical Dynamics, and the Center for Mechanical Excitability, The University of Chicago, Chicago, IL, 60637, USA. Department of Pharmacology, Vanderbilt Brain Institute, Vanderbilt University, Nashville, TN 37240, USA." About Sumit Bandekar "I am an NIH F32 postdoctoral fellow in the Araç Laboratory at the University of Chicago. I study adhesion GPCRs using structural biology perspective and I am interested in how the large multidomain extracellular region regulates receptor function. In my free time, I enjoy biking around Chicago and trying new breweries and restaurants." Sumit Bandekar on the web Araç Laboratory at UChicago X (Twitter) LinkedIn Unveiling the GPS Cleavage Mechanism in ADGRL1 with QM/MM Florian Seufert Abstract "Adhesion G-protein coupled receptors (aGPCR) are a family of 32 mammalian proteins with a defining conserved GPCR autoproteolysis inducing (GAIN) domain that catalyzes receptor self-cleavage at a GPCR proteolysis site (GPS). The autoproteolytic mechanism has been previously proposed, but remains to be validated.⁠ A previous computational study has uncovered variable flexible protein regions, whose dynamics mediate solvent-accessibility of the catalytically active GPS triad HL|S/T, however classical molecular dynamics approaches fall short of explaining the chemical reaction.⁠ Using a multiscale QM/MM approach - combining computational quantum mechanics with classical molecular dynamics - to study the GAIN domain cleavage mechanism of ADGRL1 reveals the sequence of events at the electronic level, suggesting relative energies for the individual states during the reaction, and provides insight into the structural determinants for a successful GPS cleavage exceeding the catalytically active GPS triad. By directly scanning and comparing energetic sequences of reaction steps, the most likely pathway and the individual contribution of surrounding protein residues can be elucidated. A stable π-edge contact with a conserved phenylalanine and a protonated glutamate side-chain catalyze the reactant conformation. MD simulations with the parameterized ester intermediate reveal a protonation-dependent dynamic desolvation of the GPS for subsequent ester hydrolysis by restricting water conformations. Mutational experiments on residues of interest showed that restoring the Phe-His interaction in the uncleaving ADGRB3 GAIN domain partially re-instates cleavage, while its deletion reduces cleavage in the ADGRL1 GAIN domain.⁠ We present a two-step GPS cleavage model and respective determinants of the reaction." Authors & Affiliations "Chung, Yin Kwan2, Pohl, Fabian2, Batebi, Hossein1 Sträter, Norbert3 , Langenhan, Tobias2 & Hildebrand, Peter Werner1 1 Institute of Medical Physics and Biophysics, Medical Faculty, Leipzig University, Germany 2 Rudolf Schönheimer Institute of Biochemistry, Division of General Biochemistry, Medical Faculty, Leipzig University, Germany 3 Institute of Bioanalytical Chemistry, Leipzig University, Germany" About Florian Seufert "Florian Seufert has studied Biochemistry in Leipzig, before joining the Hildebrand Lab in Leipzig for his PhD." Florian Seufert on the web LinkedIn ResearchGate < Previous Session Next Session >

GPCR Ecosystem account . 2 — Submit Your Team Details Provide names, emails, and organization information

GPCR Learning Ecosystem ✔ Full Masterclass library ✔ Terry's Pharmacology Corner ✔ Advanced GPCR courses

GPCR Learning Ecosystem ✔ Full Masterclass library ✔ Terry's Pharmacology Corner ✔ Advanced GPCR courses

GPCR Learning Ecosystem ✔ Full Masterclass library ✔ Terry's Pharmacology Corner ✔ Advanced GPCR courses

GPCR Learning Ecosystem ✔ Full Masterclass library ✔ Terry's Pharmacology Corner ✔ Advanced GPCR courses

GPCR Learning Ecosystem ✔ Full Masterclass library ✔ Terry's Pharmacology Corner ✔ Advanced GPCR courses

GPCR Learning Ecosystem ✔ Full Masterclass library ✔ Terry's Pharmacology Corner ✔ Advanced GPCR courses

GPCR Ecosystem and beyond About Monserrat Avila Zozaya "My doctoral research was focused on investigating

GPCR Learning Ecosystem ✔ Full Masterclass library ✔ Terry's Pharmacology Corner ✔ Advanced GPCR courses

GPCR Learning Ecosystem ✔ Full Masterclass library ✔ Terry's Pharmacology Corner ✔ Advanced GPCR courses

GPCR Learning Ecosystem ✔ Full Masterclass library ✔ Terry's Pharmacology Corner ✔ Advanced GPCR courses

GPCR Learning Ecosystem ✔ Full Masterclass library ✔ Terry's Pharmacology Corner ✔ Advanced GPCR courses

GPCR Learning Ecosystem ✔ Full Masterclass library ✔ Terry's Pharmacology Corner ✔ Advanced GPCR courses

Guests on The Web Maria Majellaro LinkedIn ResearchGate Ecosystem Johannes Broichhagen LinkedIn Google GPCR Learning Ecosystem ✔ Full Masterclass library ✔ Terry's Pharmacology Corner ✔ Advanced GPCR courses

GPCR Learning Ecosystem ✔ Full Masterclass library ✔ Terry's Pharmacology Corner ✔ Advanced GPCR courses

iPSC-derived cellular models and biosensor approaches for studying GPCR signaling and improving translational pharmacology workflows. < Back Using iPSC-derived models to study GPCR function April 16, 2026 10 AM - 11:30 AM EST 🔒 Watch Recordings Access the full library of recorded Masterclass sessions. Get Live Updates Be notified when new live Masterclasses are scheduled. Introduction Drug discovery pipelines increasingly depend on screening platforms designed to identify therapeutically valuable compounds. Yet despite advances in screening technologies, the translation of these discoveries into clinical success remains limited. A major factor is the continued reliance on cellular systems that do not adequately reflect the complexity of human tissues and disease biology. This Masterclass explores how induced pluripotent stem cell (iPSC)–derived cellular models and organoid systems can provide more physiologically relevant environments for studying GPCR signaling and pharmacological responses. The discussion will examine how these models are generated, how biosensor-based approaches can be integrated to monitor signaling pathways, and how such systems can support more translationally relevant drug discovery workflows. Instructor Terry Hébert has a long-standing track record in identifying molecular mechanisms that regulate the function of G protein-coupled receptors. His research has focused extensively on GPCR oligomerization, signaling complex assembly, and biased signaling. His current work investigates the ontogeny, formation, and trafficking of GPCR-based signaling complexes in order to understand how GPCR signaling pathways are organized and integrated within cells. This research examines signaling architecture both at the cell surface and within the nucleus, providing insight into how receptor signaling networks are structured and regulated. Upcoming Live Sessions

Full Agenda Adhesion GPCR workshop 2024 CINVESTAV, Mexico City, Mexico October 23-25 Download PDF Program HERE < Back to Full Agenda Leaving for City Center Coming Soon < Previous Session Next Session >

Full Agenda Adhesion GPCR workshop 2024 CINVESTAV, Mexico City, Mexico October 23-25 Download PDF Program HERE < Back to Full Agenda Leave for dinner reception Coming Soon < Previous Session Next Session >

Full Agenda Adhesion GPCR workshop 2024 CINVESTAV, Mexico City, Mexico October 23-25 Download PDF Program HERE < Back to Full Agenda Complimentary Reception dinner MENU Four Mushroom Soup Tomato, Panela Cheese, and Spinach tower with Oregano Vinaigrette Cane Sugar and Arbol Chile Lacquered Duck Monte Cristo Chocolate Cake Coffee or Tea Vegetarian option* -Mushroom-stuffed chiles on refried bean sauce- instead of the duck < Previous Session Next Session >

Full Agenda Adhesion GPCR workshop 2024 CINVESTAV, Mexico City, Mexico October 23-25 Download PDF Program HERE < Back to Full Agenda State of the Art Talk Adhesion GPCR in Mechanobiology Abstract Only Available for AGPCR24 Attendees About Tobias Langenhan "1997-2004: Medical school and Dr. med. Neuroanatomy (Würzburg, Germany); 2004-2005: M.Sc . Neuroscience (Oxford, UK); 2005-2009: D.Phil. Neuroscience (Oxford, UK); 2009-2016: Group leader, Institute of Neurophysiology (Würzburg, Germany); 2016: Heisenberg professorship (Würzburg, Germany); 2016-to date: Professor and Chair in Biochemistry (Leipzig, Germany)" Tobias Langenhan on the web Langenhan Lab LinkedIn < Previous Session Next Session >