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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
24
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pubmed:dateCreated |
1995-1-23
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pubmed:databankReference |
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pubmed:abstractText |
The transcriptional activity of c-Jun is augmented through phosphorylation at two sites by a c-Jun amino-terminal kinase (JNK). All cells express two distinct JNK activities, 46 and 55 kD in size. It is not clear which of them is the more important c-Jun kinase and how they specifically recognize c-Jun. The 46-kD form of JNK was identified as a new member of the MAP kinase group of signal-transducing enzymes, JNK1. Here, we report the molecular cloning of the 55-kD form of JNK, JNK2, which exhibits 83% identity and similar regulation to JNK1. Despite this close similarity, the two JNKs differ greatly in their ability to interact with c-Jun. JNK2 binds c-Jun approximately 25 times more efficiently than JNK1, and as a result has a lower Km toward c-Jun than JNK1. The structural basis for this difference was investigated and traced to a small beta-strand-like region near the catalytic pocket of the enzyme. Modeling suggests that this region is solvent exposed and therefore is likely to serve as a docking site that increases the effective concentration of c-Jun near JNK2. These results explain how two closely related MAP kinases can differ in their ability to recognize specific substrates and thereby elicit different biological responses.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0890-9369
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2996-3007
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8001819-Amino Acid Sequence,
pubmed-meshheading:8001819-Binding Sites,
pubmed-meshheading:8001819-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:8001819-Cell Line,
pubmed-meshheading:8001819-Cloning, Molecular,
pubmed-meshheading:8001819-Conserved Sequence,
pubmed-meshheading:8001819-Gene Expression,
pubmed-meshheading:8001819-Humans,
pubmed-meshheading:8001819-JNK Mitogen-Activated Protein Kinases,
pubmed-meshheading:8001819-Kinetics,
pubmed-meshheading:8001819-Mitogen-Activated Protein Kinase 9,
pubmed-meshheading:8001819-Mitogen-Activated Protein Kinases,
pubmed-meshheading:8001819-Models, Molecular,
pubmed-meshheading:8001819-Molecular Sequence Data,
pubmed-meshheading:8001819-Molecular Weight,
pubmed-meshheading:8001819-Protein Kinases,
pubmed-meshheading:8001819-Protein Structure, Secondary,
pubmed-meshheading:8001819-Proto-Oncogene Proteins c-jun,
pubmed-meshheading:8001819-Sequence Homology, Amino Acid,
pubmed-meshheading:8001819-Transfection,
pubmed-meshheading:8001819-Tumor Cells, Cultured
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pubmed:year |
1994
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pubmed:articleTitle |
JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation.
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pubmed:affiliation |
Department of Pharmacology, School of Medicine, La Jolla 92093-0636.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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