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Latrophilin 1 is a protein that in humans is encoded by the ADGRL1gene.[5][6] It is a member of the adhesion-GPCR family of receptors. Family members are characterized by an extended extracellular region with a variable number of protein domains coupled to a TM7 domain via a domain known as the GPCR-Autoproteolysis INducing (GAIN) domain.[7][8][9]
Function
This gene encodes a member of the latrophilin subfamily of G protein-coupled receptors (GPCR). Latrophilins may function in both cell adhesion and signal transduction. In experiments with non-human species, endogenous proteolytic cleavage within a cysteine-rich GPS (G-protein-coupled-receptor proteolysis site) domain resulted in two subunits (a large extracellular N-terminal cell adhesion subunit and a subunit with substantial similarity to the secretin/calcitonin family of GPCRs) being non-covalently bound at the cell membrane. Latrophilin-1 has been shown to recruit the neurotoxin from black widow spider venom, alpha-latrotoxin, to the synapse plasma membrane.[6]. Latrophilin-1 also binds glucose and possibly other carbohydrates because of its lectin domain.[10] It may be involved in mediating glucose and energy balance as shown recently..[10]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Hayflick JS (Jan 2001). "A family of heptahelical receptors with adhesion-like domains: a marriage between two super families". Journal of Receptor and Signal Transduction Research. 20 (2–3): 119–131. doi:10.3109/10799890009150640. PMID10994649. S2CID19919738.
^Stacey M, Yona S (2011). AdhesionGPCRs: Structure to Function (Advances in Experimental Medicine and Biology). Berlin: Springer. ISBN978-1-4419-7912-4.
^ abChhabra KH, Bathina S, Faniyan TS, Samuel DJ, Raza MU, de Souza Cordeiro LM, et al. (September 2023). "ADGRL1 is a glucose receptor involved in mediating energy and glucose homeostasis". Diabetologia. doi:10.1007/s00125-023-06010-6. PMID37712955.
Further reading
Südhof TC (2001). "alpha-Latrotoxin and its receptors: neurexins and CIRL/latrophilins". Annual Review of Neuroscience. 24: 933–962. doi:10.1146/annurev.neuro.24.1.933. PMID11520923.
Ushkaryov YA, Volynski KE, Ashton AC (April 2004). "The multiple actions of black widow spider toxins and their selective use in neurosecretion studies". Toxicon. 43 (5): 527–542. doi:10.1016/j.toxicon.2004.02.008. PMID15066411.
Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC (May 2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry". Analytical Chemistry. 76 (10): 2763–2772. doi:10.1021/ac035352d. PMID15144186.
Bjarnadóttir TK, Fredriksson R, Höglund PJ, Gloriam DE, Lagerström MC, Schiöth HB (July 2004). "The human and mouse repertoire of the adhesion family of G-protein-coupled receptors". Genomics. 84 (1): 23–33. doi:10.1016/j.ygeno.2003.12.004. PMID15203201.
External links
PDBe-KB provides an overview of all the structure information available in the PDB for Mouse Adhesion G protein-coupled receptor L1