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Distinguished immunologist, Dr Stagg is recognized for having identified the adenosine-producing enzyme Dr Stagg has served as an expert consultant in the development of adenosine-targeting drugs, several Dr Stagg is a member of the Board of Directors of BioCanRx, Canada's Immunotherapy Network, co-founder Montréal Québec Cancer Consortium The University of Montreal Hospital Research Centre Pubmed LinkedIn Dr

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Food and drinks Read More Oct 24 - 9:00 AM Session II AGPCR signaling pathways and trafficking Yuling Feng roles of AGPCRs in the nervous system Beatriz Blanco Redondo · Willem Berend Post Read More 11:10 AM Dr Direct Communication of Extracellular Region with Transmembrane Domain in a Holo-Adhesion GPCR Yuling Feng

Signaling Date & Time Saturday, November 4th / 8:40 AM Abstract Coming Soon About Sudarshan Rajagopal "Dr During his Cardiology fellowship, he trained in the lab of Dr. Robert J. Sudarshan Rajagopal on the web The Rajagopal Lab Google Scholar Pubmed LinkedIn Dr.

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Full Agenda Adhesion GPCR workshop 2024 CINVESTAV, Mexico City, Mexico October 23-25 Download PDF Program HERE < Back to Full Agenda Departure < 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 Posters Interrogating The Role Of CELSR1 (ADGRC1) In Breast Cancer Caroline Formstone Generation and characterization of collecting duct specific GPR56 knockout mice Jianxiang Xue Anti-Tumorigenic Role of Brain Angiogenesis Inhibitor 3 (BAI3) in WNT-Activated Medulloblastomas Virginea de Araujo Farias Conformational And Functional Coupling Between Extracellular and Transmembrane Regions of a Holo-Adhesion GPCR Szymon P. Kordon Deorphanization Of The Adhesion GPCRs GPR110 and GPR116 Tingzhen Shen Self-Cleavage of GPR110 SEA Domain and Its Impact on GAIN Domain Autoproteolysis Bill Huang Tethered Agonist Dependent ADGRL3 Signaling Activity In The G12/13 Pathway Júlia Rosell Endocytic Cues Determine the Signaling Profile of Adhesion GPCR ADGRL1 / Latrophilin-1 Sheila Ribalta-Mena GPR110 modulates anxiety-like behaviors and memory function in mice potentially through neuronal and neuroimmune alterations during neurodevelopment Mariam Melkumyan Interrogating The Role Of CELSR1 (ADGRC1) In Breast Cancer Caroline Formstone Abstract "Breast cancer is the most common form of cancer amongst women. Ductal carcinomas are increasingly diagnosed but identifying which will progress to invasive disease remains difficult highlighting an urgent need for new biomarkers that distinguish ductal carcinomas on this basis. Planar cell polarity (PCP) proteins contribute to tumour growth and invasion. Recent studies identify CELSR1, a key PCP gene, as a novel biomarker for early-stage breast cancer. CELSR1 is reactivated in luminal-type ductal carcinomas. The impact of CELSR1 on cancer progression, however, is unclear. Our working hypothesis is that distinct CELSR1 protein isoforms differentially regulate tissue adhesiveness by influencing the stability/plasticity of cell-cell and cell-matrix contacts. Notably, our pilot data from luminal-type breast cancer cell lines representative of breast carcinomas with lower versus higher invasive potential reveal differential enrichment of CELSR1 protein isoforms. To test the specific hypothesis that biased expression of CELSR1 isoforms will predict invasive potential of a luminal breast carcinoma we will (a) determine, via loss-of-function assays in vitro and in vivo, whether CELSR1 protein isoforms differentially influence the stability of cell-cell and/or cell-matrix adhesions to dictate breast tumour invasive mechanism (b) quantify CELSR1 isoform expression (mRNA and protein) within patient luminal carcinoma samples exhibiting non-invasive or invasive features, the latter including heterogeneous tumours with mixed pathology. Through study of known protein isoforms of CELSR1, which would be missed in gene expression microarray analyses, we hope to illuminate the prognostic potential of CELSR1 for early-stage breast cancer." Authors & Affiliations "Klena, Ladislav University of Hertfordshire" About Caroline Formstone "Cell and developmental biologist with a focus on how planar cell polarity drives complex tissue morphogenesis. I study the cell and tissue level consequences of its failure in foetal development and of its reemployment in cancer" Caroline Formstone on the web University of Hertfordshire Generation and characterization of collecting duct specific GPR56 knockout mice Jianxiang Xue Abstract "GPR56 is a multifunctional adhesin G protein-coupled receptor involved in diverse biological processes. The role of GPR56 in the kidneys has been understudied. A recent study demonstrated that GPR56 in the glomerular endothelial cells promoted diabetic kidney disease progression via regulation of eNOS. Using RNAscope in situ hybridization (ISH) for GPR56, aquaporin 2 and NKCC2 (thick ascending limb, TAL marker), we detected GPR56 mRNA highly expressed in the collecting duct and TAL of the loop of Henle with limited expression in the proximal tubule. To determine the physiological role of GPR56 in the collecting duct, we generated a collecting duct-specific GPR56 knockout (GPR56CD-KO) mouse model by crossing GPR56flox (Control) with cadherin 16 Cre mice. The deletion of GPR56 in the collecting duct was confirmed by RNAscope ISH. GPR56CD-KO mice were born at predicted Mendelian frequencies, appeared grossly indistinguishable from Con mice, and developed normally. For baseline phenotypic characterization, blood gas analysis showed no differences in blood pH, blood HCO3-, blood Na+, or blood K+ between GPR56CD-KO and control mice. Metabolic cage experiments demonstrated no differences in fluid intake, urine volume, urinary pH or urine osmolality between genotypes in baseline. 24hr water deprivation experiment showed that GPR56CD-KO mice can concentrate urine as effectively as control mice. In conclusion, we successfully generated collecting duct-specific GPR56 knockout mouse and found no defective urine concentrating ability in GPR56CD-KO mice. This mouse model will be useful to delineate the collecting duct-specific role of GPR56 for renal function, including acid-base regulation." Authors & Affiliations "Hailey Steichen, Krystin Eaton, Teagan Yan, and Nathan Zaidman; Department of Biochemistry and Molecular Biology, University of New Mexico" About Jianxiang Xue "I am a postdoctoral researcher working in the Department of Biochemistry and Molecular Biology, University of New Mexico. I earned my PhD degree in Biomedical Sciences from the University of South Florida. During my graduate studies, using various transgenic mouse models and expertise in intestinal and renal physiology, I systematically characterized the function of sodium/hydrogen exchanger 3 in the intestine and kidneys for fluid and electrolyte homeostasis and acid-base balance. My predoctoral work was supported by an American Heart Association fellowship. Since staring my postdoctoral training, I have continued to develop my expertise to answer fundamental questions on adhesion GPCR in renal physiology and pathology. In my free time, I enjoy reading, workouts, and hiking." Jianxiang Xue on the web Zaidman Physiology Lab Anti-Tumorigenic Role of Brain Angiogenesis Inhibitor 3 (BAI3) in WNT-Activated Medulloblastomas Virginea de Araujo Farias Abstract Only available for AGPCR 24 Workshop Attendees Authors & Affiliations "Van Meir, Erwin G. University of Alabama at Birmingham" About Virginea de Araujo Farias "Brain Angiogenesis Inhibitor (BAI) proteins are members of group VII of the adhesion G protein-coupled receptor (aGPCR) family. BAI1-3 are highly expressed in the brain, where they participate in synaptogenesis and synapse maintenance. In cancers, BAI1-3 expression can be lost through epigenetic silencing, copy number loss or truncating mutations. In medulloblastomas (MB), BAI3 (ADGRB3) expression is specifically reduced in the WNT-activated group (WNT-MB), but not in the other three molecular groups. WNT pathway activation in WNT-MB is driven by mutations of the CTNNB1 gene, activating ß-catenin-dependent signaling; however, no interactions between BAI3 and the WNT signaling pathway have been described so far. MAGI3, a PDZ-containing scaffolding protein is known to downregulate WNT signaling by interacting with ß-catenin in gliomas, but it is unknown whether this involves BAI3. To explore a possible connection between BAI3 and ß-catenin signaling through MAGI3 in WNT-MB, we probed for potential protein-protein interactions using co-IP experiments. We found an interaction between BAI3 and MAGI3 in mouse brain lysates. Therefore, we hypothesize that re-expression of BAI3 in WNT-MB cells will restrain ß-catenin activity through the formation of a BAI3/MAGI3/ß-catenin complex, reducing their tumorigenic properties. To test this hypothesis, we created WNT-like MB cell lines stably expressing tet-on wild-type BAI3 or a BAI3 lacking the C-terminal PDZ-binding motif (PBM). We will present the effects of BAI3 re-expression on WNT-MB cells oncogenic properties and signaling." Virginea de Araujo Farias on the web Google Scholar Conformational And Functional Coupling Between Extracellular and Transmembrane Regions of a Holo-Adhesion GPCR Szymon P. Kordon Abstract "Adhesion G Protein-Coupled Receptors (aGPCRs) are key cell-adhesion molecules involved in numerous physiological functions. aGPCRs have large multi-domain extracellular regions (ECR) that mediate cell adhesion and play roles in transmitting extracellular signals to the inside of the cell. Ligand binding and mechanical force applied on the ECR regulate receptor function. However, how the ECR communicates with the seven-pass transmembrane domain (7TM) remains elusive, because the relative orientation and dynamics of the ECR and 7TM within a holoreceptor is unclear. Here, we describe the cryo-EM reconstruction of an aGPCR, Latrophilin3/ADGRL3, and reveal that the conserved GAIN domain, that directly precedes 7TM, adopts a parallel orientation to the membrane and has constrained movement. Single-molecule FRET experiments unveil three slow-exchanging FRET states of the ECR relative to the 7TM within the holoreceptor. GAIN-targeted antibodies, and cancer-associated mutations at the GAIN-7TM interface, alter holoreceptor conformations, and modulate downstream receptor signaling. Altogether, this data demonstrates conformational and functional coupling between the ECR and 7TM, suggesting an ECR-mediated mechanism for aGPCR activation." Authors & Affiliations "Cechova Kristina (3), Bandekar Sumit J.(1, 2), Leon Katherine (1, 2), Dutka Przemysław (1, 4), Siffer Gracie (3), Kossiakoff Anthony A. (1), Vafabakhsh Reza (3), Araç Demet (1, 2) 1. Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL, USA; 2. Neuroscience Institute, Institute for Biophysical Dynamics, and Center for Mechanical Excitability, The University of Chicago, Chicago, IL, USA; 3. Department of Molecular Biosciences, Northwestern University, Evanston, IL, USA; 4. Current affiliation: Department of Structural Biology, Genentech, South San Francisco, CA, USA" About Szymon P. Kordon "I am a postdoctoral scholar in the Araç Lab at The University of Chicago, studying the structure and function of aGPCRs. Utilizing synthetic antibody fragments, I aim to understand better the structural basis of the aGPCRs activation and signaling and to characterize ECR-mediated signal transduction at the molecular level." Szymon P. Kordon on the web Araç Laboratory at UChicago Deorphanization Of The Adhesion GPCRs GPR110 and GPR116 Tingzhen Shen Abstract Only available for AGPCR 24 Workshop Attendees Authors & Affiliations "Frank E. Kwarcinski, Gregory G. Tall (University of Michigan, Ann Arbor)" About Tingzhen Shen "A graduate student from Tall Lab, department of Pharmacology, University of Michigan, Ann Arbor." Tingzhen Shen on the web University of Michigan Self-Cleavage of GPR110 SEA Domain and Its Impact on GAIN Domain Autoproteolysis Bill Huang Abstract Only available for AGPCR 24 Workshop Attendees Authors & Affiliations "Hee-Yong Kim, Laboratory of Molecular Signaling, National Institute on Alcohol Abuse and Alcoholism, National Institutes of Health, Rockville, MD, USA" About Bill Huang "Researcher" Bill Huang on the web LinkedIn Tethered Agonist Dependent ADGRL3 Signaling Activity In The G12/13 Pathway Júlia Rosell Abstract Only available for AGPCR 24 Workshop Attendees Authors & Affiliations "Regmi, Rajesh (1), Perry-Hauser, Nicole A. (2), Javitch, Jonathan A. (2), Mathiasen, Signe (1) (1) Department of Biomedical Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark. (2) Department of Psychiatry and Molecular Pharmacology and Therapeutics, Columbia University Vagelos College of Physicians and Surgeons, New York, USA; Division of Molecular Therapeutics, New York State Psychiatric Institute, New York, USA" About Júlia Rosell "I am a first-year PhD student with two years of experience in the adhesion GPCR field. I completed my Master’s thesis on ADGRL3, where I conducted research involving mammalian cell cultures and techniques such as BRET assays and gene expression assays. Currently, my research focuses on the intracellular signaling of ADGRL3 from a single-molecule perspective and investigating how the binding of extracellular transsynaptic ligands modulates ADGRL3 activity, aiming to elucidate their interplay." Júlia Rosell on the web LinkedIn Endocytic Cues Determine the Signaling Profile of Adhesion GPCR ADGRL1 / Latrophilin-1 Sheila Ribalta-Mena Abstract Only available for AGPCR 24 Workshop Attendees Authors & Affiliations " Hernández-Aranda Judith 2, Correoso-Braña Kerlys 1, Vialou Vincent 3, Leduc Richard 4, Olivares-Reyes Jesús Alberto 2, Boucard Antony A1. 1 Department of Cell Biology, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (Cinvestav-IPN), México City, México. 2 Department of Biochemistry, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (Cinvestav-IPN), México City, México. 3 Sorbonne Université, Inserm, CNRS, Neurosciences Paris Seine, Paris, France. 4 Department of Physiology and Pharmacology, Université de Sherbrooke, Sherbrooke, Canada " About Sheila Ribalta-Mena " Cell Biology PhD student " Sheila Ribalta-Mena on the web CINVESTAV ResearchGate LinkedIn GPR110 modulates anxiety-like behaviors and memory function in mice potentially through neuronal and neuroimmune alterations during neurodevelopment Mariam Melkumyan Abstract "GPR110, an adhesion G protein coupled receptor (GPCR), is widely expressed in developing brains but diminishes in adult stage except in the hippocampus, a region involved in learning and memory. Ligand-induced GPR110 signaling stimulates neurogenesis and synaptogenesis during development, and the absence of the ligand-induced signaling causes object recognition and spatial memory deficits in adulthood and increased neuroinflammatory responses. Nevertheless, the role of GPR110 signaling in behavioral consequences has not been fully explored. This study aimed to understand the effects of GPR110 on mouse behaviors in relation to neurodevelopmental and neuroimmune gene and protein expression. Anxiety and memory function were tested using both male and female mice at 5-6 month of age. GPR110 knockout (KO) mice displayed trends for increased anxiety-like behaviors in the elevated plus maze test and in the open field test. Memory tests, including the novel object test and the radial 8-arm maze showed worsened spatial and reference memory in the GPR110 KO mice compared to wildtype mice. The y-maze showed a significant sex by genotype interactions with GPR110 KO male mice having increased number of correct alterations and errors, while the GPR110 KO females had fewer correct alterations and errors. RNAseq data indicated significantly impaired developmental gene expression for neuronal differentiation, axonogenesis, and synaptogenesis, as well as altered neuroinflammatory marker expression in GPR110 KO mouse brains. Further studies exploring the protein expression and neural activity of these mouse brain will give insight on the mechanism underlying the behavioral consequences associated with the GPR110 receptor. " Authors & Affiliations "Joel Toro, Bill Huang, Hee-Yong Kim Laboratory of Molecular Signaling, National Institute of Alcohol Abuse and Alcoholism, NIH" About Mariam Melkumyan "Mariam Melkumyan is a postdoctoral fellow at the Laboratory of Molecular Signaling studying the role of GPR110 in neurotransmission and neuroimmune activity involved in learning and memory, anxiety, and alcohol use. Mariam, originally from Armenia, completed her bachelor's degree in Neuroscience at American University in Washington, DC and her dual-title PhD in Neuroscience and Clinical and Translational Sciences at Penn State College of Medicine in Hershey, PA. Mariam started her postdoctoral training in February 2024 and is hoping to become an academic professor and mentor the next generation of scientists." Mariam Melkumyan on the web LinkedIn Google Scholar < Previous Session Next Session >

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

Showcase your creativity in the AGPCR24 Logo Contest! Submit your design to represent the Adhesion GPCR Workshop and inspire our global community. LOGO CONTEST Adhesion GPCR workshop 2024 CINVESTAV, Mexico City, Mexico October 23-25 Register Rules for the logo contest Design must be based on “Alebrijes” [ah-leh-bree-hez], which are chimeric creatures from Mexican folklore AND contain adhesion GPCRs Avoid copyrighted material unless a CC BY / open-use license has been acquired or generated (Adobe Stock, etc). The Consortium must be free to use the design. Requirements: Resolution 300 ppi max, JPEG/TIFF/EPS/PNG/PDF formats, 5MB max Open to all adhesion GPCR community members. Artist-scientists must be registered to attend the adhesion GPCR workshop 2024 in Mexico City. The contest deadline is August 15th, 2024, 11:59 PM CST (designs received after the deadline will not be considered) Designs or inquiries should be sent to this email The prize for the selected design will include free registration and more! 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.

Your go-to guide for attending AGPCR24. Find essential travel information, from transportation and accommodation tips to local insights, to help you make the most of your trip and enjoy a smooth, stress-free conference experience. TRAVELING TIPS Adhesion GPCR workshop 2024 CINVESTAV, Mexico City, Mexico October 23-25 Register DO's and DONT's for travelers in Mexico Mexico travel advice *Travelers are encouraged to consult their country's embassy advisories as they may differ from the one posted above. The Canadian embassy provides a comprehensive list. We highly suggest reserving accommodations in the city's center as the housing around the venue is scarce, and some may not be suitable for a convenient stay. Do not hesitate to contact us if you have inquiries regarding the neighborhood of your choice. We suggest the following neighborhoods: Roma Norte, Juárez, Zona Rosa, Condesa, Cuauhtémoc, San Rafael Apart from the numerous Airbnb options in these neighborhoods, here are our recommendations for affordable hotels in order of preference: 1. Hotel Carlota : An industrial chic experience at economical pricing. It can include breakfasts. 2. Hotel Exe Suites Reforma 3. Hotel Maria Cristina : Old School “hacienda”-type hotel. 4. Hotel Laila 5. City Express by Marriott EBC Reforma 6. Hoteles PF Zona Rosa MAP AIR TRAVEL Mexico City is accessible by two major airports. Transportation options, approximate travel times, and approximate fares to and from the airports are listed. Fares are subject to change. Airfare and other travel arrangements are the full responsibility of aGPCR Workshop 2024 attendees. Aeropuerto Internacional de la Ciudad de México (AICM) Benito Juárez is located 15 km from the “Angel de la Independencia” and 13 km from Cinvestav. This airport is the best option for international travel. Time/Distance : Approximate 35-minute drive. Taxis : Taxis are available at the lower levels (outside of baggage claim) at each terminal. Fares are based on traffic conditions, but an average fare is $20-$30. Subway : The subway is only available at Terminal 1. If your flight arrives at Terminal 2, there is a shuttle to Terminal 1. At the subway station you can purchase a “Movilidad Integrada” card in order to access public transportation (subway, metrobus, bikes, bus, etc). Information from public transportation can be followed through Google Maps or City Mapper apps. Uber and Didi apps : Uber type applications are available in Mexico City and a safe option for transportation. Aeropuerto Internacional Felipe Ángeles (AIFA) is located 53 km from the “Angel de la Independencia” and 33 km from Cinvestav. Time/Distance : Approximate 60-minute drive. Taxis : Taxis are available at the lower levels (outside of baggage claim) at each terminal. Fares are based on traffic conditions, but an average fare is $30-$50. Public Transportation : We recommend taking a shuttle (available for travelers) from AIFA to AICM Terminal 1. TRAVEL & VISA INFORMATION We look forward to welcoming attendees. Please check if you need a visa or permit to enter Mexico. After identifying that a visa or permit is needed, foreign travelers should contact their country's Mexican Embassy Consular Section. To request a Letter of Invitation for visa purposes, contact us. MONEY EXCHANGE Mexican pesos are the currency of Mexico. Reliable exchange booths are available at airports, banks, and hotels. However, many businesses accept credit/debit cards. POSTER PRINTING Poster printing is the full responsibility of aGPCR Workshop 2024 attendees. Office Depot and Office Max offer services for poster printing. Close to Cinvestav, on “Instituto Politécnico Nacional” avenue, there are several small local businesses offering poster printing services. The average fare for poster printing is $10-$12. SIM CARD AND WIFI SIM cards can be easily purchased at the airport and Oxxo stores around the city. The average fare is $10-$12. Public Wi-Fi is available around the city, including at airports and subway stations, and just outside of Cinvestav. FOOD RESTRICTIONS Please share any food restrictions you might have (allergies, dietary, etc). We will try to accommodate you as best we can. GETTING TO THE VENUE UBER is the most recommended as it is a highly economical and safe way to reach Cinvestav from your housing accommodation. We recommend carpooling with others to reduce individual costs and to be environmentally friendly. Typical costs are $8 USD one way ($2 USD / person carpooling with four people). 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 Logo Contest Enter our logo contest for a chance to have your design represent the upcoming event.

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 >

Funding source Oral presentations Extended deadline: August 1st Speaker name indicated in bold and underlined

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 >

Full Agenda Adhesion GPCR workshop 2024 CINVESTAV, Mexico City, Mexico October 23-25 Download PDF Program HERE < Back to Full Agenda Complimentary Lunch < 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 VIII Physiological and pathological roles of AGPCRs in the periphery ADGRG1/GPR56 regulates survival of terminally differentiated CD8+ T cells Cheng-Chih Hsiao Adhesion GPCR GPR116/Adgrf5 controls a lineage of anti-thermogenic adipocytes with implications for adaptive thermogenesis during prolonged cold exposure Anastasia Georgiadi ADGRF5-mediated regulation of cardiac health and disease Douglas Tilley ADGRG1/GPR56 regulates survival of terminally differentiated CD8+ T cells Cheng-Chih Hsiao Abstract Only available for AGPCR 24 Attendees Authors & Affiliations "Cheng-Chih Hsiao1,2, Hendrik J. Engelenburg1, Joost Smolders1,3, and Jörg Hamann1,2 1Department of Neuroimmunology, Netherlands Institute for Neuroscience, Amsterdam, The Netherlands; 2Department of Experimental Immunology, Amsterdam institute for Immunology and Infectious diseases, Amsterdam University Medical Center, Amsterdam, The Netherlands; 3MS center ErasMS, Departments of Neurology and Immunology, Erasmus Medical Center, Rotterdam, The Netherlands" About Cheng-Chih Hsiao "2012-2015: PhD in Immunology, University of Amsterdam; 2015-2019: Postdoctoral researcher, Amsterdam UMC; 2019-2022: Senior postdoctoral researcher, Netherlands Institute for Neuroscience; 2022 - present: Researcher associate, Netherlands Brain Bank" Cheng-Chih Hsiao on the web LinkedIn ReseachGate Adhesion GPCR GPR116/Adgrf5 controls a lineage of anti-thermogenic adipocytes with implications for adaptive thermogenesis during prolonged cold exposure Anastasia Georgiadi Abstract Only available for AGPCR 24 Attendees Authors & Affiliations "El Merabhi Rabih1*, Karagiannakou Vasiliki1*, Kardinal Ronja2, Jäckstein Michelle3 Yvonne, Kumar Jha Ankush1, Krokidi Sissy Thodou1, Wachten Dagmar2, Heeren Jörg3, Herzig Stephan1, Georgiadi Anastasia1 *equal contributions , Institutions : 1. Institute for Diabetes and Cancer, Helmholtz Centre Munich, Germany, 2. Institute of Innate Immunity, University Hospital Bonn, University of Bonn, 3. Centre for Experimental Medicine, Institute for Biocehmistry and Molecular Cell Biology, University Medical Center Hamburg-Eppendorf" About Anastasia Georgiadi "Head of Junior Group Endocrine Pharmacology, Institute of Diabetes and Cancer (IDC). Professional Background Since 2021 Group Leader, Institute for Diabetes and Cancer, Helmholtz Diabetes Centre, Munich 2018 - 2021 Project Team Leader, Institute for Diabetes and Cancer, Helmholtz Diabetes Centre, Munich 2015 - 2018 Postdoctoral fellow, Department of Adipose Tissue Biology, Institute for Diabetes and Cancer, Helmholtz Diabetes Centre, Munich 2012 - 2015 Postdoctoral fellow, Department of Cell and Molecular Biology, Karolinska Institute, Sweden" Anastasia Georgiadi on the web Endocrine Pharmacology Google Scholar ADGRF5-mediated regulation of cardiac health and disease Douglas Tilley Abstract Only available for AGPCR 24 Attendees About Douglas Tilley "Research in the Tilley laboratory focuses primarily upon aspects of GPCR regulation of cardiac function, inflammation and remodeling during HF or following acute cardiac injury. Much of this work centered on elucidating novel mechanisms by which β-adrenergic receptors impact cardiac structure and function, and has evolved to encompass their roles in regulating immune cell response to acute cardiac injury or chronic stress. Additionally, the lab has begun to investigate potential roles for previously unrecognized cardiac-expressed GPCRs in the regulation of physiologic/pathologic function in the heart in an effort to uncover novel therapeutic directions for HF, including adhesion GPCRs (AGPCRs). In all, research in the Tilley lab spans molecular pharmacology to pathophysiology studies focused primarily in the cardiovascular realm." Douglas Tilley on the web Lewis Katz School of Medicine at Temple University < Previous Session Next Session >