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Proc Natl Acad Sci U S A. 1999 May 25;96(11):6371-6.

Interaction between RGS7 and polycystin.

Author information

1
Laboratory of Molecular and Developmental Neuroscience, Massachusetts General Hospital, Harvard Medical School, Boston, MA 02114, USA.

Abstract

Regulators of G protein signaling (RGS) proteins accelerate the intrinsic GTPase activity of certain Galpha subunits and thereby modulate a number of G protein-dependent signaling cascades. Currently, little is known about the regulation of RGS proteins themselves. We identified a short-lived RGS protein, RGS7, that is rapidly degraded through the proteasome pathway. The degradation of RGS7 is inhibited by interaction with a C-terminal domain of polycystin, the protein encoded by PKD1, a gene involved in autosomal-dominant polycystic kidney disease. Furthermore, membranous expression of C-terminal polycystin relocalized RGS7. Our results indicate that rapid degradation and interaction with integral membrane proteins are potential means of regulating RGS proteins.

PMID:
10339594
PMCID:
PMC26888
DOI:
10.1073/pnas.96.11.6371
[Indexed for MEDLINE]
Free PMC Article

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