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Signalling pathways involved in multisite phosphorylation of the transcription factor ATF‐2
Author(s) -
Morton Simon,
Davis Roger J,
Cohen Philip
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.07.031
Subject(s) - phosphorylation , p38 mitogen activated protein kinases , kinase , phosphorylation cascade , microbiology and biotechnology , mapk/erk pathway , mapk14 , mitogen activated protein kinase kinase , mitogen activated protein kinase , protein kinase a , map kinase kinase kinase , map2k7 , chemistry , ask1 , cyclin dependent kinase 2 , protein phosphorylation , biology
The multisite phosphorylation of the transcription factor ATF‐2 was investigated using transformed embryonic fibroblasts from wild‐type mice and mice deficient in c‐Jun N‐terminal kinases (JNK)1 and 2, and in the presence and absence of inhibitors of p38 mitogen‐activated protein kinase (p38 MAPK) and the classical MAP kinase cascade. In wild‐type cells, p38 MAPK and extracellular signal‐regulated protein kinase (ERK)1/2 were not rate limiting for the phosphorylation of Thr69, Thr71 or Ser90. In JNK‐deficient cells, p38 MAPK substituted for JNK partially in the phosphorylation of Thr69 and p38 MAPK or ERK1/2 in the phosphorylation of Thr71. JNK was the only MAP kinase that phosphorylated Ser90 under the conditions examined.