Signalling pathways involved in multisite phosphorylation of the transcription factor ATF-2

Simon Morton, Roger J. Davis, Philip Cohen (Lead / Corresponding author)

    Research output: Contribution to journalArticle

    73 Citations (Scopus)

    Abstract

    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.

    Original languageEnglish
    Pages (from-to)177-183
    Number of pages7
    JournalFEBS Letters
    Volume572
    Issue number1-3
    DOIs
    Publication statusPublished - 13 Aug 2004

    Keywords

    • AP-1, activating protein 1
    • ATF-2, activating transcription factor-2
    • CRE, cyclic AMP-response element
    • E1A, early adenovirus protein 1A
    • EGF, epidermal growth factor
    • ERK, extracellular signal-regulated protein kinase
    • GST, glutathione S-transferase

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