Interaction between RGS7 and polycystin.
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.
Mesh Terms:
Amino Acid Sequence, B-Lymphocytes, Binding Sites, Cysteine Endopeptidases, GTP-Binding Proteins, Gene Library, Humans, Molecular Sequence Data, Multienzyme Complexes, Polycystic Kidney, Autosomal Dominant, Proteasome Endopeptidase Complex, Protein Biosynthesis, Proteins, RGS Proteins, Recombinant Proteins, Saccharomyces cerevisiae, Sequence Alignment, Sequence Homology, Amino Acid, TRPP Cation Channels, Transcription, Genetic, Ubiquitins
Amino Acid Sequence, B-Lymphocytes, Binding Sites, Cysteine Endopeptidases, GTP-Binding Proteins, Gene Library, Humans, Molecular Sequence Data, Multienzyme Complexes, Polycystic Kidney, Autosomal Dominant, Proteasome Endopeptidase Complex, Protein Biosynthesis, Proteins, RGS Proteins, Recombinant Proteins, Saccharomyces cerevisiae, Sequence Alignment, Sequence Homology, Amino Acid, TRPP Cation Channels, Transcription, Genetic, Ubiquitins
Proc. Natl. Acad. Sci. U.S.A.
Date: May. 25, 1999
PubMed ID: 10339594
View in: Pubmed Google Scholar
Download Curated Data For This Publication
10331
Switch View:
- Interactions 3