Interaction between RGS7 and Polycystin

Regulators of G protein signaling (RGS) proteins accelerate the intrinsic GTPase activity of certain Gα 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 protei...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1999-05, Vol.96 (11), p.6371-6376
Main Authors: Kim, Emily, Arnould, Thierry, Sellin, Lorenz, Benzing, Thomas, Comella, Natalia, Kocher, Olivier, Tsiokas, Leonidas, Sukhatme, Vikas P., Walz, Gerd
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
B-Lymphocytes - metabolism
Binding Sites
Biological Sciences
Cysteine Endopeptidases - metabolism
Disease
Enzymes
Gene expression regulation
Gene Library
GTP-Binding Proteins - chemistry
GTP-Binding Proteins - metabolism
Half lives
Humans
Kidneys
Medical research
Medical sciences
Molecular Sequence Data
Multienzyme Complexes - metabolism
Pests
Plasmids
Polycystic Kidney, Autosomal Dominant - genetics
Polycystic Kidney, Autosomal Dominant - metabolism
Proteasome Endopeptidase Complex
Protein Biosynthesis
Proteins
Proteins - chemistry
Proteins - genetics
Proteins - metabolism
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
RGS Proteins
Saccharomyces cerevisiae
Sequence Alignment
Sequence Homology, Amino Acid
Transcription, Genetic
TRPP Cation Channels
Ubiquitins - metabolism
Yeasts
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Summary:Regulators of G protein signaling (RGS) proteins accelerate the intrinsic GTPase activity of certain Gα 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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.96.11.6371