G alpha (q):RGS dissociates to inactive G alpha (q)

Stable Identifier
R-HSA-8982026
Type
Reaction [dissociation]
Species
Homo sapiens
Compartment
plasma membrane
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G alpha (q):RGS dissociates to inactive G alpha (q)
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G Protein Coupled Receptors (GPCR) sense extracellular signals and activate different Guanine nucleotide binding proteins (G proteins). Upon activation, GPCRs can replace the GDP with GTP in the alpha subunit of G proteins. GTP binding modifies the conformation of G alpha proteins and activates them. The Regulator of G protein Signalling (RGS) are GTPase Accelerating Proteins (GAPs) that can directly inhibit the G alpha subunit activity. There are at least 25 different types of RGS proteins known. Several of these RGS proteins (1, 2, 3, 4, 5, 8, 13, 16, 17, 18, 19, 21) can bind and stabilize the transition state of Guanine nucleotide binding protein G(q) subunit alpha class (GNAQ/GNA11/GNA14/GNA15). Subsequently, the RGS domain in the complex facilitates the hydrolyses of G alpha (q):GTP to G alpha (q):GDP. Following this, the complex dissociates releasing inactive G alpha (q) (Neubig & Siderovski 2002, Kach et al. 2012). The primary function of G alpha (q) is activation of phospholipase C beta thereby triggering phosphoinositide hydrolysis, calcium mobilization and protein kinase C activation.

Literature References
PubMed ID Title Journal Year
18434541 Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits

Soundararajan, M, Willard, FS, Kimple, AJ, Turnbull, AP, Ball, LJ, Schoch, GA, Gileadi, C, Fedorov, OY, Dowler, EF, Higman, VA, Hutsell, SQ, Sundström, M, Doyle, DA, Siderovski, DP

Proc. Natl. Acad. Sci. U.S.A. 2008
12120503 Regulators of G-protein signalling as new central nervous system drug targets

Neubig, RR, Siderovski, DP

Nat Rev Drug Discov 2002
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Orthologous Events
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Authored
Varusai, TM  (2017-07-27)
Reviewed
Siderovski, D  (2018-09-03)
Created
Varusai, TM  (2017-03-15)
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