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EMBO J. 1995 May 1;14(9):2014-9.

Intramolecular signal transduction in c-Jun.

Author information

1
European Molecular Biology Laboratory, Differentiation Program, Heidelberg, Germany.

Abstract

The DNA-binding activity of c-Jun is determined by the phosphorylation state of a cluster of threonine and serine residues located near its COOH-terminus. We have analyzed the events that lead to c-Jun activation via dephosphorylation of these sites in response to phorbol esters. Our results indicate that COOH-terminal dephosphorylation is an indirect consequence of a separate phosphorylation event targeted to the NH2-terminus of c-Jun. Thus, the activation of c-Jun DNA-binding potential, caused by COOH-terminal dephosphorylation, may not require the regulation of the kinase/phosphatase system that brings about this change, but rather an alteration in the accessibility of the COOH-terminal phosphoacceptor sites of c-Jun.

PMID:
7744008
PMCID:
PMC398301
[Indexed for MEDLINE]
Free PMC Article

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