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      Intramolecular signal transduction in c-Jun.

      The EMBO Journal
      Amino Acid Sequence, Binding Sites, DNA, genetics, metabolism, HeLa Cells, Humans, Molecular Sequence Data, Mutation, Phosphorylation, Proto-Oncogene Proteins c-jun, Signal Transduction

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          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.

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          Author and article information

          Journal
          7744008
          398301
          10.1002/j.1460-2075.1995.tb07193.x

          Chemistry
          Amino Acid Sequence,Binding Sites,DNA,genetics,metabolism,HeLa Cells,Humans,Molecular Sequence Data,Mutation,Phosphorylation,Proto-Oncogene Proteins c-jun,Signal Transduction

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