ADGRG heterodimer translocates to plasma membrane

Stable Identifier
Reaction [omitted]
Homo sapiens
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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
23695165 Sticky signaling--adhesion class G protein-coupled receptors take the stage

Langenhan, T, Hamann, J, Aust, G

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

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

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

Piao, X, Mehta, P

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

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

Genes Cells 2004
Orthologous Events
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