ADGRG heterodimer translocates to plasma membrane

Stable Identifier
R-HSA-9614273
Type
Reaction [omitted]
Species
Homo sapiens
Compartment
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Mature ADGRG6 is expressed at the plasma membrane as a non-covalently associated heterodimer of the N- and C terminal fragments (Moriguchi et al, 2004; Arac et al, 2012; reviewed in Langenhan et al, 2013; Mehta et al, 2017). In addition to cleavage at the GPS site, ADGRG6 may additionally be cleaved in the trans-Golgi network by a furin-like protease at an S2 site upstream of the GPS site. This cleavage yields a soluble N-terminal-most subfragment that may have roles in non cell autonomous signaling or contribute to regulation of ADGRG6 activation/inactivation (Moriguchi et al, 2004; reviewed in Langenhan et al, 2013).

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

Langenhan, T, Aust, G, Hamann, J

Sci Signal 2013
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
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