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IDENTIFICATION OF AN ONCOPROTEIN-RESPONSIVE AND UV-RESPONSIVE PROTEIN-KINASE THAT BINDS AND POTENTIATES THE C-JUN ACTIVATION DOMAIN
Author(s): HIBI M, LIN AN, SMEAL T, MINDEN A, KARIN M
Source: GENES & DEVELOPMENT    Volume: 7    Issue: 11    Pages: 2135-2148    Published: NOV 1993  
Times Cited: 1,470     References: 60     
Abstract: The activity of c-Jun is regulated by phosphorylation. Various stimuli including transforming oncogenes and UV light, induce phosphorylation of serines 63 and 73 in the amino-terminal activation domain of c-Jun and thereby potentiate its trans-activation function. We identified a serine/threonine kinase whose activity is stimulated by the same signals that stimulate the amino-terminal phosphorylation of c-Jun. This novel c-Jun amino-terminal kinase (JNK), whose major form is 46 kD, binds to a specific region within the c-Jun trans-activation domain and phosphorylates serines 63 and 73. Phosphorylation results in dissociation of the c-Jun-JNK complex. Mutations that disrupt the kinase-binding site attenuate the response of c-Jun to Ha-Ras and UV. Therefore the binding of JNK to c-Jun is of regulatory importance and suggests a mechanism through which protein kinase cascades can specifically modulate the activity of distinct nuclear targets.
Document Type: Article
Language: English
Addresses:
1. UNIV CALIF SAN DIEGO, SCH MED, CTR MOLEC GENET, DEPT PHARMACOL, LA JOLLA, CA 92093 USA
2. UNIV CALIF SAN DIEGO, SCH MED, CTR MOLEC GENET, DEPT BIOL, LA JOLLA, CA 92093 USA
Publisher: COLD SPRING HARBOR LAB PRESS, 1 BUNGTOWN RD, PLAINVIEW, NY 11724
Subject Category: Cell Biology; Developmental Biology; Genetics & Heredity
IDS Number: MF828
ISSN: 0890-9369
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