Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1992-2-18
|
| pubmed:abstractText |
The primary structure of bovine rhodopsin kinase (RK), which phosphorylates light-activated rhodopsin (Rho*), terminates with the amino acid sequence Cys558-Val-Leu-Ser561, a motif that has been shown to direct the isoprenylation and alpha-carboxyl methylation of many proteins (e.g. p21Ha-ras). Transient expression of RK in COS-7 cells revealed the presence of two immunoreactive protein species. Consistent with RK being modified by isoprenylation, interconversion of these two species was dependent upon isoprenoid biosynthesis in the cells. Moreover, a serine substitution for Cys558 resulted in a single RK species whose migration on sodium dodecyl sulfate-polyacrylamide gels was identical to that of RK from cells treated with mevinolin, an inhibitor of 3-hydroxy-3-methylglutaryl-coenzyme A reductase and, thus, of isoprenoid biosynthesis. This finding indicates that isoprenylation of RK requires Cys558. The electrophoretic mobility of isoprenylated RK synthesized in COS-7 cells was identical to that of RK from bovine rod outer segments, suggesting that RK is isoprenylated in vivo. RK was determined to be modified by a farnesyl moiety and alpha-carboxyl-methylated. A time course of Rho* phosphorylation revealed that non-processed RK is approximately 4-fold less active than wild-type RK. This is the first demonstration of isoprenylation/alpha-carboxyl methylation of a protein kinase, and suggests that these modifications markedly influence enzymatic activity in vivo.
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Eye Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/G-Protein-Coupled Receptor Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Methionine,
http://linkedlifedata.com/resource/pubmed/chemical/Mevalonic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
25
|
| pubmed:volume |
267
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1422-5
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:1730692-Amino Acid Sequence,
pubmed-meshheading:1730692-Animals,
pubmed-meshheading:1730692-Blotting, Western,
pubmed-meshheading:1730692-Cattle,
pubmed-meshheading:1730692-Cell Line,
pubmed-meshheading:1730692-Eye Proteins,
pubmed-meshheading:1730692-G-Protein-Coupled Receptor Kinase 1,
pubmed-meshheading:1730692-Glutathione Transferase,
pubmed-meshheading:1730692-Kinetics,
pubmed-meshheading:1730692-Methionine,
pubmed-meshheading:1730692-Methylation,
pubmed-meshheading:1730692-Mevalonic Acid,
pubmed-meshheading:1730692-Molecular Sequence Data,
pubmed-meshheading:1730692-Molecular Weight,
pubmed-meshheading:1730692-Mutagenesis, Site-Directed,
pubmed-meshheading:1730692-Protein Kinases,
pubmed-meshheading:1730692-Protein Processing, Post-Translational,
pubmed-meshheading:1730692-Recombinant Fusion Proteins,
pubmed-meshheading:1730692-Rod Cell Outer Segment,
pubmed-meshheading:1730692-Transfection
|
| pubmed:year |
1992
|
| pubmed:articleTitle |
Isoprenylation of a protein kinase. Requirement of farnesylation/alpha-carboxyl methylation for full enzymatic activity of rhodopsin kinase.
|
| pubmed:affiliation |
Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina 27710.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|