Linked Life Data

7629115

Source:http://linkedlifedata.com/resource/pubmed/id/7629115

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
1995-9-5
pubmed:abstractText
Recoverin (Rv) is a myristoylated Ca(2+)-binding protein present primarily in bovine photoreceptors. It represents a newly identified family of neuronal specific Ca(2+)-binding proteins that includes neurocalcin, hippocalcin, and guanylyl cyclase-activating protein. To investigate the function of Rv in photoreceptors, we identified proteins that bind immobilized Rv in a Ca(2+)-dependent manner. Rhodopsin kinase (RK), interphotoreceptor retinoid-binding protein, and tubulin interact with Rv in the presence of Ca2+. The importance of the Rv/RK interaction was further characterized. RK, purified using immobilized Rv as an affinity matrix, catalyzed the light-dependent and Ca(2+)-independent incorporation of phosphates into rhodopsin when reconstituted with urea-stripped rod outer segment membranes. When only a small fraction (0.04%) of rhodopsin was photolyzed, as many as 700 phosphates were incorporated per photolyzed rhodopsin, a phenomenon known as "high gain" phosphorylation. When recoverin was added, the activity of RK became sensitive to free Ca2+, with EC50 = 3 microM. The N-terminal myristoyl residue of Rv enhances the inhibitory effect of Rv and introduces cooperativity to the Ca(2+)-dependent inhibition of rhodopsin phosphorylation. Rv neither interacts with other members of the G-protein-coupled receptor kinase family such as beta-adrenergic receptor kinase 1 nor inhibits beta-adrenergic receptor kinase 1 activity. The specific and Ca(2+)-dependent Rv/RK interaction is necessary for the inhibitory effect of Rv on rhodopsin phosphorylation and may play an important role in photoreceptor light adaptation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18060-6
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:7629115-Amino Acid Sequence, pubmed-meshheading:7629115-Animals, pubmed-meshheading:7629115-Calcium, pubmed-meshheading:7629115-Calcium-Binding Proteins, pubmed-meshheading:7629115-Catalysis, pubmed-meshheading:7629115-Cattle, pubmed-meshheading:7629115-Chromatography, Affinity, pubmed-meshheading:7629115-Eye Proteins, pubmed-meshheading:7629115-G-Protein-Coupled Receptor Kinase 1, pubmed-meshheading:7629115-Hippocalcin, pubmed-meshheading:7629115-Lipoproteins, pubmed-meshheading:7629115-Molecular Sequence Data, pubmed-meshheading:7629115-Nerve Tissue Proteins, pubmed-meshheading:7629115-Phosphorylation, pubmed-meshheading:7629115-Photoreceptor Cells, pubmed-meshheading:7629115-Protein Kinase Inhibitors, pubmed-meshheading:7629115-Protein Kinases, pubmed-meshheading:7629115-Recoverin, pubmed-meshheading:7629115-Rod Cell Outer Segment, pubmed-meshheading:7629115-Urea
pubmed:year
1995
pubmed:articleTitle
Ca(2+)-dependent interaction of recoverin with rhodopsin kinase.
pubmed:affiliation
Department of Biochemistry, University of Washington, Seattle 98195, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.