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

FEBS Letters

Marshall, Chris J.¹  Gomez, Nestor²  Ashworth, Alan¹  Saito, Yuji²  Campbell, David G.²  Cohen, Philip² 

[1] Chester Realty Laboratories, Institute of Cancer Research, London SW3 6JB, UK;MRC Protein Phosphorylation Unit, Department of Biochemistry, University of Dundee, Dundee DD1 4HN, UK

关键词: MAP kinase;    MAP kinase kinase;    Growth factor;    Phosphopeptide;    Amino acid sequence;   

DOI  :  10.1016/0014-5793(94)80252-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown