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PMID: 8917514 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

RGS-r, a retinal specific RGS protein, binds an intermediate conformation of transducin and enhances recycling.

Chen CK, Wieland T, Simon MI

Abstract

G proteins regulate intracellular signaling by coupling a cycle of guanine nucleotide binding and hydrolysis to transient changes of cellular functions. The mechanisms that control the recycling of transducin, the "pacesetting" G protein that regulates mammalian phototransduction, are unclear. We show that a novel retinal specific RGS-motif protein specifically binds to an intermediate conformation involved in GTP hydrolysis by transducin and accelerates phosphate release and the recycling of transducin. This specific interaction further rationalizes the kinetics of the phototransduction cascade and provides a general hypothesis to explain the mechanism of interaction of RGS proteins with other G proteins.

MeSH Terms
Amino Acid Sequence Animals Carrier Proteins/chemistry,isolation & purification,metabolism Cattle DNA Primers Eye Proteins/chemistry,isolation & purification,metabolism GTP Phosphohydrolases/metabolism GTP-Binding Proteins/metabolism Guanosine Triphosphate/metabolism Male Mice Molecular Sequence Data Organ Specificity Polymerase Chain Reaction Protein Binding Protein Conformation RGS Proteins Rats Recombinant Proteins/biosynthesis,isolation & purification,metabolism Retina/metabolism Rod Cell Outer Segment/metabolism Sequence Homology, Amino Acid Transducin/isolation & purification,metabolism
Chemicals
Carrier Proteins DNA Primers Eye Proteins RGS Proteins RGS16 protein Recombinant Proteins Guanosine Triphosphate GTP Phosphohydrolases GTP-Binding Proteins Transducin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Chen C K
Division of Biology, California Institute of Technology, Pasadena 91125, USA.
Wieland T
Simon M I
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24 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1996-11-12
Pages
12885-9
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC24015
Subset
IM
Grants
NIA NIH HHS · AG 12288 · United States
Databases
GENBANK
U72881
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