A G protein gamma subunit-like domain shared between RGS11 and other RGS proteins specifies binding to Gbeta5 subunits.

Regulators of G protein signaling (RGS) proteins act as GTPase-activating proteins (GAPs) toward the alpha subunits of heterotrimeric, signal-transducing G proteins. RGS11 contains a G protein gamma subunit-like (GGL) domain between its Dishevelled/Egl-10/Pleckstrin and RGS domains. GGL domains are also found in RGS6, RGS7, RGS9, and the Caenorhabditis elegans protein ...
EGL-10. Coexpression of RGS11 with different Gbeta subunits reveals specific interaction between RGS11 and Gbeta5. The expression of mRNA for RGS11 and Gbeta5 in human tissues overlaps. The Gbeta5/RGS11 heterodimer acts as a GAP on Galphao, apparently selectively. RGS proteins that contain GGL domains appear to act as GAPs for Galpha proteins and form complexes with specific Gbeta subunits, adding to the combinatorial complexity of G protein-mediated signaling pathways.
Mesh Terms:
Amino Acid Sequence, Animals, Binding Sites, Brain, COS Cells, Caenorhabditis elegans, Cattle, Consensus Sequence, Conserved Sequence, GTP-Binding Proteins, GTPase-Activating Proteins, Humans, Macromolecular Substances, Mice, Molecular Sequence Data, Organ Specificity, Protein Binding, Protein Biosynthesis, Proteins, RNA, Messenger, Rats, Recombinant Proteins, Retina, Sequence Alignment, Sequence Homology, Amino Acid, Spodoptera, Transcription, Genetic, Transfection
Proc. Natl. Acad. Sci. U.S.A.
Date: Oct. 27, 1998
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