Autocleavage of ADGRG6

Stable Identifier
R-HSA-9614271
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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ADGRG6, also known as GPR126, is a member of the adhesion class of G-protein coupled receptors (aGPCRs). aGPCRs are characterized by a 7 transmembrane-spanning domain that couples to G-protein signaling and an extracellular N-terminal extension that mediates cell-cell or cell-matrix adhesion (reviewed in Langenhan et al, 2013). Like most aGPCRs, ADGRG6 is subject to autocatalytic processing during maturation, yielding a C-terminal fragment containing the 7-TM region, and an N-terminal fragment containing the extracellular region. Cleavage occurs at the conserved GPCR proteolytic site (GPS), part of the larger GPCR autoproteolysis-inducing (GAIN) domain (Moriguchi et al, 2004; Arac et al, 2012). As with other aGPCRs, these two domains remain associated in a heterodimer at the plasma membrane where they mediate signaling and cell adhesion (Moriguchi et al 2004; Arac et al, 2012; Lin et al, 2004; reviewed in Langenhan et al, 2013; Mehta et al, 2017).

Literature References
PubMed ID Title Journal Year
23695165 Sticky signaling--adhesion class G protein-coupled receptors take the stage

Langenhan, T, Aust, G, Hamann, J

Sci Signal 2013
22333914 A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis

Araç, D, Boucard, AA, Bolliger, MF, Nguyen, J, Soltis, SM, Südhof, TC, Brunger, AT

EMBO J. 2012
27859941 Adhesion G-protein coupled receptors and extracellular matrix proteins: Roles in myelination and glial cell development

Mehta, P, Piao, X

Dev. Dyn. 2017
15189448 DREG, a developmentally regulated G protein-coupled receptor containing two conserved proteolytic cleavage sites

Moriguchi, T, Haraguchi, K, Ueda, N, Okada, M, Furuya, T, Akiyama, T

Genes Cells 2004
15150276 Autocatalytic cleavage of the EMR2 receptor occurs at a conserved G protein-coupled receptor proteolytic site motif

Lin, HH, Chang, GW, Davies, JQ, Stacey, M, Harris, J, Gordon, S

J. Biol. Chem. 2004
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
endopeptidase activity of ADGRG6 [endoplasmic reticulum membrane]
Physical Entity
Activity
Orthologous Events
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Created