Linked Life Data

10722682

Source:http://linkedlifedata.com/resource/pubmed/id/10722682

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2000-4-27
pubmed:abstractText
The C-terminal domain of G protein-coupled receptor kinases (GRKs) consists of a conserved region and a variable region, and the variable region has been shown to direct the membrane translocation of cytosolic enzymes. The present work has revealed that the C-terminal domain may also be involved in kinase-receptor interaction that is primarily mediated by the conserved region. Truncation of the C-terminal domain or deletion of the conserved region in this domain of GRK2 resulted in a complete loss of its ability to phosphorylate rhodopsin and in an obvious decrease in its sensitivity to receptor-mediated phosphorylation of a peptide substrate. On the contrary, deletion of the betagamma subunit binding region in the C-terminal domain of GRK2 did not significantly alter the ability of the enzyme to phosphorylate rhodopsin. In addition, the recombinant proteins that represent the C-terminal domain and the conserved region of GRK2 could inhibit GRK2-mediated phosphorylation of rhodopsin and receptor-mediated activation of GRK2 but not GRK2-mediated phosphorylation of the peptide substrate. Furthermore, the conserved region as well as the C-terminal domain could directly bind rhodopsin in vitro. These results indicate that the C-terminal domain, or more precisely, the conserved region of this domain, is important for enzyme-receptor interaction and that this interaction is required for GRK2 to catalyze receptor phosphorylation.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
275
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8469-74
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:10722682-Adrenergic beta-Antagonists, pubmed-meshheading:10722682-Amino Acid Sequence, pubmed-meshheading:10722682-Animals, pubmed-meshheading:10722682-Cattle, pubmed-meshheading:10722682-Conserved Sequence, pubmed-meshheading:10722682-Cyclic AMP-Dependent Protein Kinases, pubmed-meshheading:10722682-Escherichia coli, pubmed-meshheading:10722682-G-Protein-Coupled Receptor Kinase 2, pubmed-meshheading:10722682-Mutagenesis, pubmed-meshheading:10722682-Peptide Fragments, pubmed-meshheading:10722682-Phosphorylation, pubmed-meshheading:10722682-Protein Binding, pubmed-meshheading:10722682-Receptors, Adrenergic, beta, pubmed-meshheading:10722682-Recombinant Proteins, pubmed-meshheading:10722682-Rhodopsin, pubmed-meshheading:10722682-Sequence Deletion, pubmed-meshheading:10722682-beta-Adrenergic Receptor Kinases, pubmed-meshheading:10722682-rho GTP-Binding Proteins
pubmed:year
2000
pubmed:articleTitle
Interaction between the conserved region in the C-terminal domain of GRK2 and rhodopsin is necessary for GRK2 to catalyze receptor phosphorylation.
pubmed:affiliation
Shanghai Institute of Biochemistry, Shanghai 200031, People's Republic of China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't