| Mechanistic basis for the failure of cone transducin to translocate: why cones are never blinded by light. | |
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MedLine Citation:
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PMID: 20484624 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The remarkable ability of our vision to function under ever-changing conditions of ambient illumination is mediated by multiple molecular mechanisms regulating the light sensitivity of rods and cones. One such mechanism involves massive translocation of signaling proteins, including the G-protein transducin, into and out of the light-sensitive photoreceptor outer segment compartment. Transducin translocation extends the operating range of rods, but in cones transducin never translocates, which is puzzling because cones typically function in much brighter light than rods. Using genetically manipulated mice in which the rates of transducin activation and inactivation were altered, we demonstrate that, like in rods, transducin translocation in cones can be triggered when transducin activation exceeds a critical level, essentially saturating the photoresponse. However, this level is never achieved in wild-type cones: their superior ability to tightly control the rates of transducin activation and inactivation, responsible for avoiding saturation by light, also accounts for the prevention of transducin translocation at any light intensity. |
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Authors:
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Ekaterina S Lobanova; Rolf Herrmann; Stella Finkelstein; Boris Reidel; Nikolai P Skiba; Wen-Tao Deng; Rebecca Jo; Ellen R Weiss; William W Hauswirth; Vadim Y Arshavsky |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: The Journal of neuroscience : the official journal of the Society for Neuroscience Volume: 30 ISSN: 1529-2401 ISO Abbreviation: J. Neurosci. Publication Date: 2010 May |
Date Detail:
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Created Date: 2010-05-20 Completed Date: 2010-06-04 Revised Date: 2011-09-26 |
Medline Journal Info:
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Nlm Unique ID: 8102140 Medline TA: J Neurosci Country: United States |
Other Details:
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Languages: eng Pagination: 6815-24 Citation Subset: IM |
Affiliation:
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Albert Eye Research Institute, Duke University, Durham, North Carolina 27710, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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3',5'-Cyclic-GMP Phosphodiesterases
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metabolism Aging / genetics, metabolism Animals Basic-Leucine Zipper Transcription Factors / deficiency Electroretinography / methods Eye Proteins G-Protein-Coupled Receptor Kinase 1 / deficiency GTP-Binding Protein alpha Subunits / metabolism GTP-Binding Protein gamma Subunits / metabolism Gene Expression Regulation / genetics Light Light Signal Transduction / genetics, physiology* Membrane Proteins / deficiency Mice Mice, Inbred C57BL Mice, Knockout Models, Biological Protein Transport / genetics, physiology RGS Proteins / deficiency Retinal Cone Photoreceptor Cells / metabolism* Retinal Rod Photoreceptor Cells / metabolism Transducin / metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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EY072224/EY/NEI NIH HHS; EY08571/EY/NEI NIH HHS; EY10336/EY/NEI NIH HHS; EY11123/EY/NEI NIH HHS; EY13729/EY/NEI NIH HHS; EY5722/EY/NEI NIH HHS; P30 EY005722-24/EY/NEI NIH HHS; R01 EY010336-19/EY/NEI NIH HHS; R01 EY011123-14/EY/NEI NIH HHS; R01 EY012224-08/EY/NEI NIH HHS; U10 EY013729-05/EY/NEI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Basic-Leucine Zipper Transcription Factors; 0/Eye Proteins; 0/GTP-Binding Protein alpha Subunits; 0/GTP-Binding Protein gamma Subunits; 0/Membrane Proteins; 0/Nrl protein, mouse; 0/R9AP protein, mouse; 0/RGS Proteins; 0/regulator of g-protein signaling 9; EC 2.7.1.37/Grk1 protein, mouse; EC 2.7.11.14/G-Protein-Coupled Receptor Kinase 1; EC 3.1.4.35/3',5'-Cyclic-GMP Phosphodiesterases; EC 3.6.1.-/Transducin |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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