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Intramolecular signal transduction in c‐Jun.
Author(s) -
Papavassiliou A.G.,
Treier M.,
Bohmann D.
Publication year - 1995
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1995.tb07193.x
Subject(s) - biology , signal transduction , transduction (biophysics) , genetics , microbiology and biotechnology , biochemistry
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.