Published November 12, 1996
| Published
Journal Article
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RGS-r, a retinal specific RGS protein, binds an intermediate conformation of transducin and enhances recycling
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 "pace-setting" 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.
Additional Information
© 1996 by the National Academy of Sciences Contributed by Melvin I. Simon, September 26, 1996 Data deposition: The sequence reported in this paper has been deposited in the GenBank data base (accession no. U72881). C.-K.C. and T.W. contributed equally to this work. We thank Dr. Wolfgang Baehr for mouse retinal cDNA library and members of the Simon lab and, in particular, Bo Yu for stimulating discussion. This work was supported from the National Institute on Aging (AG 12288). T.W. is the recipient of a fellowship from the Deutsche Forschungsgemeinschaft. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.Attached Files
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Additional details
- PMCID
- PMC24015
- Eprint ID
- 784
- Resolver ID
- CaltechAUTHORS:CHEpnas96b.825
- AG 12288
- NIH
- Deutsche Forschungsgemeinschaft (DFG)
- Created
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2005-09-30Created from EPrint's datestamp field
- Updated
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2022-10-05Created from EPrint's last_modified field