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Protein Domain : IPR008376

Description  The chaperones Ric-8, also known as Synembryns, specifically bind and fold nascent G alpha proteins prior to G protein heterotrimer formation, promoting their stability and activity. Mammalian Chaperone Ric-8A assists the folding of GNAI1, GNAO1, GNA13 and GNAQ but doesn't fold Gα proteins GNAS nor GNAL [ ]. It also acts as a guanine nucleotide exchange factor (GEF) for Gα proteins by stimulating exchange of bound GDP for free GTP [, , , , ]. Chaperone Ric-8B binds and folds nascent Gα proteins, GNAS and GNAL, prior to G protein heterotrimer formation, promoting their association with the plasma membrane [, ]. The invertebrate homologues bind some, but not all, nascent Gα proteins [].These proteins that positively regulate synaptic transmission. They are actively required to maintain proper activity of the Go to Gq G-protein signalling network, which regulates neurotransmitter secretion in Caenorhabditis elegans by controlling the production and consumption of diacylglycerol [ ]. In addition to its role in the adult nervous system, synembryn is required to regulate a subset of centrosome movements in the early C. elegans embryo [].The protein appears to be concentrated in the cytoplasm of neurons. However, unlike other protein components of the Go-Gq signalling network, synembryn appears to be more concentrated in the cell soma than in axonal processes throughout the nervous system [ ]. C. elegans synembryn reduction of function mutants exhibit partial embryonic lethality []. Name  Chaperone Ric-8 A/B
Short Name  Chaperone_Ric-8_A/B Type  Domain
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