Latrophilin 1 is a protein that in humans is encoded by the ADGRL1gene.[1][2] 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.[3][4][5]
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.[2]
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Südhof TC (2001). "alpha-Latrotoxin and its receptors: neurexins and CIRL/latrophilins". Annual Review of Neuroscience. 24: 933–62. doi:10.1146/annurev.neuro.24.1.933. PMID11520923.
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Kreienkamp HJ, Zitzer H, Gundelfinger ED, Richter D, Bockers TM (Oct 2000). "The calcium-independent receptor for alpha-latrotoxin from human and rodent brains interacts with members of the ProSAP/SSTRIP/Shank family of multidomain proteins". The Journal of Biological Chemistry. 275 (42): 32387–90. doi:10.1074/jbc.C000490200. PMID10964907.
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): 2763–72. doi:10.1021/ac035352d. PMID15144186.
Bjarnadóttir TK, Fredriksson R, Höglund PJ, Gloriam DE, Lagerström MC, Schiöth HB (Jul 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.
