The threonine residues in MAP kinase kinase 1 phosphorylated by MAP kinase in vitro are also phosphorylated in nerve growth factor-stimulated rat phaeochromocytoma (PC12) cells

Yuji Saito, Nestor Gomez, David G. Campbell, Alan Ashworth, Chris J. Marshall, Philip Cohen

    Research output: Contribution to journalArticlepeer-review

    35 Citations (Scopus)

    Abstract

    The residues on MAP kinase kinase-1 (MAPKK1) phosphorylated by MAP kinase in vitro have been identified as Thr-291 and Thr-385. Both threonines are phosphorylated in PC12 cells and the 32P-labelling of each residue increases after stimulation with nerve growth factor (NGF). The results establish that MAPKK1 is a physiological substrate for MAP kinase. The two active forms of MAPKK that are resolved by Mono Q chromatography of PC12 cell extracts are both phosphorylated at Thr-291 and Thr-385, demonstrating that neither species is the MAPKK2 isoform which lacks Thr-291.

    Original languageEnglish
    Pages (from-to)119-124
    Number of pages6
    JournalFEBS Letters
    Volume341
    Issue number1
    DOIs
    Publication statusPublished - 14 Mar 1994

    Keywords

    • Amino acid sequence
    • Growth factor
    • MAP kinase
    • MAP kinase kinase
    • Phosphopeptide

    Fingerprint Dive into the research topics of 'The threonine residues in MAP kinase kinase 1 phosphorylated by MAP kinase in vitro are also phosphorylated in nerve growth factor-stimulated rat phaeochromocytoma (PC12) cells'. Together they form a unique fingerprint.

    Cite this