作者: A.G. Papavassiliou , M. Treier , D. Bohmann
DOI: 10.1002/J.1460-2075.1995.TB07193.X
关键词: Cell biology 、 Phosphatase 、 Biochemistry 、 Threonine 、 Biology 、 Phosphorylation 、 Kinase 、 Dephosphorylation 、 Serine 、 Signal transduction 、 Phosphorylation cascade
摘要: The DNA-binding activity of c-Jun is determined by the phosphorylation state a cluster threonine and serine residues located near its COOH-terminus. We have analyzed events that lead to activation via dephosphorylation these sites in response phorbol esters. Our results indicate COOH-terminal an indirect consequence separate event targeted NH2-terminus c-Jun. Thus, potential, caused dephosphorylation, may not require regulation kinase/phosphatase system brings about this change, but rather alteration accessibility phosphoacceptor