Regulatory mechanisms involved in modulating RGS function |
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Authors: | G Jean-Baptiste Z Yang M T Greenwood |
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Institution: | (1) Department of Anatomy and Cell Biology, McGill University, 3640 University St., Room W315, Montreal, Quebec, H3A 2B2, Canada;(2) Department of Medicine, Polypeptide Laboratory, McGill University, Montreal, Quebec, Canada |
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Abstract: | Regulator of G-Protein Signaling (RGS) refers to a conserved 120–125 amino acid motif that was first identified by its ability
to negatively regulate G-Protein-Coupled Receptor (GPCR) signalling. Mechanistically, RGSs were found to regulate GPCR responses
by binding to and stimulating the GTPase activity of the receptor-activated GTP-bound G α subunits. There are now over 25
mammalian RGSs containing proteins that are reported to carry out a variety of functions, many of which are unrelated to GPCR
signalling. RGS proteins range in size from small proteins that contain little more than an RGS box to very large proteins
that contain a variety of domains. The selectivity of function of the RGS proteins is attributable to the divergence of the
RGS sequences as well as the presence of a variety of functional motifs, which allow them to interact with other proteins.
Here we focus on the RGSs that are involved in modulating GPCR signalling by reviewing the diversity of the mechanisms involved
in regulating these RGSs.
Received 9 February 2006; received after revision 4 May 2006; accepted 22 May 2006 |
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Keywords: | RGS G-protein coupled receptor (GPCR) interacting proteins yeast endogenous expression |
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