Intramolecular signal transduction in c-Jun.
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.
Papavassiliou
A G
AG
European Molecular Biology Laboratory, Differentiation Program, Heidelberg, Germany.
Treier
M
M
Bohmann
D
D
D000595:Amino Acid Sequence; D001665:Binding Sites; D004247:DNA / Q000235:genetics / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D008969:Molecular Sequence Data; D009154:Mutation; D010766:Phosphorylation; D016755:Proto-Oncogene Proteins c-jun / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction
D016755:Proto-Oncogene Proteins c-jun; D004247:DNA