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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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B-Lymphocytes / metabolism
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Binding Sites
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Cysteine Endopeptidases / metabolism
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GTP-Binding Proteins / chemistry
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GTP-Binding Proteins / metabolism
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Gene Library
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Humans
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Molecular Sequence Data
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Multienzyme Complexes / metabolism
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Polycystic Kidney, Autosomal Dominant / genetics
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Polycystic Kidney, Autosomal Dominant / metabolism
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Proteasome Endopeptidase Complex
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Protein Biosynthesis
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Proteins / chemistry
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Proteins / genetics*
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Proteins / metabolism*
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RGS Proteins*
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Saccharomyces cerevisiae
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Sequence Alignment
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Sequence Homology, Amino Acid
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TRPP Cation Channels
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Transcription, Genetic
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Ubiquitins / metabolism
Substances
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Multienzyme Complexes
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Proteins
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RGS Proteins
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RGS7 protein, human
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Recombinant Proteins
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TRPP Cation Channels
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Ubiquitins
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polycystic kidney disease 1 protein
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Cysteine Endopeptidases
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Proteasome Endopeptidase Complex
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GTP-Binding Proteins
Associated data
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GENBANK/AF090116
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GENBANK/AF090117