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  • Title: Two RGS proteins that inhibit Galpha(o) and Galpha(q) signaling in C. elegans neurons require a Gbeta(5)-like subunit for function.
    Author: Chase DL, Patikoglou GA, Koelle MR.
    Journal: Curr Biol; 2001 Feb 20; 11(4):222-31. PubMed ID: 11250150.
    Abstract:
    BACKGROUND: Gbeta proteins have traditionally been thought to complex with Ggamma proteins to function as subunits of G protein heterotrimers. The divergent Gbeta(5) protein, however, can bind either Ggamma proteins or regulator of G protein signaling (RGS) proteins that contain a G gamma-like (GGL) domain. RGS proteins inhibit G protein signaling by acting as Galpha GTPase activators. While Gbeta(5) appears to bind RGS proteins in vivo, its association with Ggamma proteins in vivo has not been clearly demonstrated. It is unclear how Gbeta(5) might influence RGS activity. In C. elegans there are exactly two GGL-containing RGS proteins, EGL-10 and EAT-16, and they inhibit Galpha(o) and Galpha(q) signaling, respectively. RESULTS: We knocked out the gene encoding the C. elegans Gbeta(5) ortholog, GPB-2, to determine its physiological roles in G protein signaling. The gpb-2 mutation reduces the functions of EGL-10 and EAT-16 to levels comparable to those found in egl-10 and eat-16 null mutants. gpb-2 knockout animals are viable, and exhibit no obvious defects beyond those that can be attributed to a reduction of EGL-10 or EAT-16 function. GPB-2 protein is nearly absent in eat-16; egl-10 double mutants, and EGL-10 protein is severely diminished in gpb-2 mutants. CONCLUSIONS: Gbeta(5) functions in vivo complexed with GGL-containing RGS proteins. In the absence of Gbeta(5), these RGS proteins have little or no function. The formation of RGS-Gbeta(5) complexes is required for the expression or stability of both the RGS and Gbeta(5) proteins. Appropriate RGS-Gbeta(5) complexes regulate both Galpha(o) and Galpha(q) proteins in vivo.
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