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Title:
Mitogen-Activated Protein Kinase Kinase 7 is an Activator of the c-Jun NH2-terminal Kinase
Authors:
Tournier, Cathy; Whitmarsh, Alan J.; Cavanagh, Julie; Barrett, Tamera; Davis, Roger J.
Affiliation:
AA(Howard Hughes Medical Institute and Program in Molecular Medicine, Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, MA 01605), AB(Howard Hughes Medical Institute and Program in Molecular Medicine, Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, MA 01605), AC(Howard Hughes Medical Institute and Program in Molecular Medicine, Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, MA 01605), AD(Howard Hughes Medical Institute and Program in Molecular Medicine, Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, MA 01605), AE(Howard Hughes Medical Institute and Program in Molecular Medicine, Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, MA 01605)
Publication:
Proceedings of the National Academy of Sciences of the United States of America, Volume 94, Issue 14, 1997, pp.7337-7342
Publication Date:
07/1997
Origin:
JSTOR; PNAS
DOI:
10.1073/pnas.94.14.7337
Bibliographic Code:
1997PNAS...94.7337T

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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