Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH 2 -terminal kinase
Cathy Tournier, Alan J. Whitmarsh, Julie Cavanagh, Tamera Barrett, Roger J. Davis
Abstract
Cathy Tournier, Alan J. Whitmarsh, Julie Cavanagh, Tamera Barrett, Roger J. Davis
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.
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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.
Key concepts: MAP kinase kinase kinase, MAP2K7, Mitogen-activated protein kinase kinase, Cyclin-dependent kinase 9, ASK1, c-Raf, Cyclin-dependent kinase 4, Cyclin-dependent kinase 2