Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain.

• M Hibi

• A Lin

• T Smeal

• A Minden

• M Karin

抄録

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.

収録刊行物

• Genes & Development

  Genes & Development 7 (11), 2135-2148, 1993-11

  Cold Spring Harbor Laboratory

キーワード

• Developmental Biology
• Genetics

詳細情報

• CRID: 1361699993736515328
• NII論文ID: 80007345530
• DOI: 10.1101/gad.7.11.2135
• ISSN: 15495477
• ISSN: 08909369
• ISSN: http://id.crossref.org/issn/08909369
• Web Site: https://syndication.highwire.org/content/doi/10.1101/gad.7.11.2135
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