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Volume 272, Number 40, Issue of October 3, 1997 pp. 24751-24754
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

COMMUNICATION:
Identification of c-Jun NH2-terminal Protein Kinase (JNK)-activating Kinase 2 as an Activator of JNK but Not p38

(Received for publication, June 12, 1997, and in revised form, August 11, 1997)

Xianghuai Lu , Shino Nemoto and Anning Lin

From the Department of Pathology, Division of Molecular and Cellular Pathology, the University of Alabama at Birmingham, Birmingham, Alabama 35294

c-Jun NH2-terminal protein kinase (JNK), a distant member of the mitogen-activated protein (MAP) kinase family, regulates gene expression in response to various extracellular stimuli. JNK is activated by JNK-activating kinase 1 (JNKK1), a dual specificity protein kinase that phosphorylates JNK on threonine 183 and tyrosine 185 residues. Here we show that JNKK2, a novel member of the MAP kinase kinase family, was phosphorylated and activated by MEKK1, a MAP kinase kinase kinase in the JNK signaling cascade. JNKK2 activity was also stimulated by constitutively active forms of Rac and Cdc42Hs, members of the Rho small GTP-binding protein family. Unlike JNKK1 that activates both JNK and p38 MAP kinases, JNKK2 stimulated only JNK. Transient transfection assays demonstrated that JNKK2 potentiated the stimulation of c-Jun transcriptional activity by MEKK1. The existence of multiple JNK-activating kinases may contribute to the specificity of the JNK signaling cascade.


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