Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain.
説明
<jats:p>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.</jats:p>
収録刊行物
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- Genes & Development
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Genes & Development 7 (11), 2135-2148, 1993-11
Cold Spring Harbor Laboratory
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詳細情報 詳細情報について
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- CRID
- 1361699993736515328
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- NII論文ID
- 80007345530
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- ISSN
- 15495477
- 08909369
- http://id.crossref.org/issn/08909369
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- データソース種別
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