GAIN domain

The GAIN domain is a protein domain found in a number of cell surface receptors, including adhesion-GPCRs and polycystic kidney disease proteins PKD1 and PKD2. The domain is involved in the self-cleavage of these transmembrane receptors has been shown to be crucial for their function (ref needed). Point mutations within the GAIN domain of PKD1 and GPR56 are known to cause polycystic kidney disease and polymicrogyria, respectively.

GPCR-Autoproteolsis INducing (GAIN) domain, rat latrophilin 4DLQ mediates autocatalytic cleavage of adhesion GPCRs

[1][2][3]

References

  1. Araç, D; Boucard, AA; Bolliger, MF; Nguyen, J; Soltis, SM; Südhof, TC; Brunger, AT (Feb 14, 2012). "A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis.". The EMBO Journal 31 (6): 1364–78. doi:10.1038/emboj.2012.26. PMC 3321182. PMID 22333914.
  2. Lin, HH; Chang, GW; Davies, JQ; Stacey, M; Harris, J; Gordon, S (Jul 23, 2004). "Autocatalytic cleavage of the EMR2 receptor occurs at a conserved G protein-coupled receptor proteolytic site motif.". The Journal of Biological Chemistry 279 (30): 31823–32. doi:10.1074/jbc.M402974200. PMID 15150276.
  3. Chang, GW; Stacey, M; Kwakkenbos, MJ; Hamann, J; Gordon, S; Lin, HH (Jul 17, 2003). "Proteolytic cleavage of the EMR2 receptor requires both the extracellular stalk and the GPS motif.". FEBS Letters 547 (1-3): 145–50. doi:10.1016/S0014-5793(03)00695-1. PMID 12860403.