Abstract
The c-Jun NH2-terminal kinase (JNK) group of mitogen-activated protein (MAP) kinases is activated by phosphorylation on Thr and Tyr. Here we report the molecular cloning of a new member of the mammalian MAP kinase kinase group (MKK7) that functions as an activator of JNK. In vitro protein kinase assays demonstrate that MKK7 phosphorylates and activates JNK, but not the p38 or extracellular signal-regulated kinase groups of MAP kinase. Expression of MKK7 in cultured cells causes activation of the JNK signal transduction pathway. MKK7 is therefore established to be a novel component of the JNK signal transduction pathway.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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CHO Cells
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Cloning, Molecular
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Cricetinae
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Gene Expression Regulation, Enzymologic*
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Humans
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JNK Mitogen-Activated Protein Kinases*
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MAP Kinase Kinase 4
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MAP Kinase Kinase 7
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Mitogen-Activated Protein Kinase Kinases
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Molecular Sequence Data
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Protein Kinases / genetics*
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Protein Kinases / metabolism
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Sequence Alignment
Substances
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Protein Kinases
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JNK Mitogen-Activated Protein Kinases
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MAP Kinase Kinase 4
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MAP Kinase Kinase 7
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MAP2K7 protein, human
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Mitogen-Activated Protein Kinase Kinases
Associated data
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GENBANK/AF003199
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GENBANK/U93030
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GENBANK/U93031
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GENBANK/U93032