Journal article
Recoverin: a Calcium Sensitive Activator of Retinal Rod Guanylate Cyclase
Science (American Association for the Advancement of Science), v 251(4996), pp 915-918
22 Feb 1991
PMID: 1672047
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Vertebrate retinal photoreceptors recover from photoexcitation-induced hydrolysis of guanosine 3′, 5′-monophosphate (cyclic GMP) by resynthesizing cyclic GMP, which reopens cation channels that have been closed by light. Activation of guanylate cyclase by light-induced depletion of cytosolic calcium is a key event in this recovery process. This cyclase has now been shown to be regulated by a 23-kilodalton calcium binding protein. The protein is present in both rod and cone photoreceptors and was named recoverin because it promotes recovery of the dark state. The amino acid sequence of recoverin exhibits three potential calcium binding sites (EF hands). That recoverin binds calcium was confirmed with calcium-45 and by observing calcium-induced changes in its tryptophan fluorescence. Recoverin activated guanylate cyclase when free calcium was lowered from 450 to 40 nM, an effect that was blocked by an antibody to recoverin. Thus, guanylate cyclase in retinal rods is stimulated during recovery by the calcium-free form of recoverin. A comparison of recoverin with other calcium binding proteins reveals that it may represent, along with the protein visinin, a family of proteins that are regulated by submicromolar calcium concentrations.
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Details
- Title
- Recoverin: a Calcium Sensitive Activator of Retinal Rod Guanylate Cyclase
- Creators
- Alexander M. Dizhoor - Lomonosov Moscow State UniversitySanghamitra Ray - Stanford UniversitySantosh Kumar - University of WashingtonGreg Niemi - University of WashingtonMaribeth Spencer - University of WashingtonDoane Brolley - University of WashingtonKenneth A. Walsh - University of WashingtonPaul P. Philipov - Lomonosov Moscow State UniversityJames B. Hurley - University of WashingtonLubert Stryer - Stanford University
- Publication Details
- Science (American Association for the Advancement of Science), v 251(4996), pp 915-918
- Publisher
- American Association for the Advancement of Science (AAAS)
- Number of pages
- 4
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Neurobiology and Anatomy
- Web of Science ID
- WOS:A1991EY62900037
- Scopus ID
- 2-s2.0-0025825054
- Other Identifier
- 991022035258004721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology