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PubMed · 10339594

Interaction between RGS7 and polycystin.

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

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Amino Acid SequenceB-LymphocytesBinding SitesCysteine EndopeptidasesGTP-Binding ProteinsGene LibraryHumansMolecular Sequence DataMultienzyme ComplexesPolycystic Kidney, Autosomal DominantProteasome Endopeptidase ComplexProtein BiosynthesisProteinsRGS ProteinsRecombinant ProteinsSaccharomyces cerevisiaeSequence AlignmentSequence Homology, Amino AcidTRPP Cation ChannelsTranscription, GeneticUbiquitinsJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, P.H.S.

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E Kim, T Arnould, L Sellin, T Benzing, N Comella, O Kocher, L Tsiokas, V P Sukhatme, G Walz. 1999-05-25. Interaction between RGS7 and polycystin.. https://doi.org/10.1073/pnas.96.11.6371

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