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Interaction between RGS7 and polycystin.

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.

SUBMITTER: Kim E

PROVIDER: S-EPMC26888 | biostudies-literature | 1999 May

REPOSITORIES: biostudies-literature

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Interaction between RGS7 and polycystin.

Kim E E Arnould T T Sellin L L Benzing T T Comella N N Kocher O O Tsiokas L L Sukhatme V P VP Walz G G

Proceedings of the National Academy of Sciences of the United States of America 19990501 11

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 in ...[more]

PMID: 10339594

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