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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
Author(s) -
Saito Yuji,
Gomez Nestor,
Campbell David G.,
Ashworth Alan,
Marshall Chris J.,
Cohen Philip
Publication year - 1994
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 - 10.1016/0014-5793(94)80252-1
Subject(s) - map2k7 , mitogen activated protein kinase kinase , mapk14 , map kinase kinase kinase , cyclin dependent kinase 9 , cyclin dependent kinase 2 , phosphorylation , kinase , mitogen activated protein kinase , mapkapk2 , mapk7 , chemistry , biochemistry , ask1 , protein kinase a , microbiology and biotechnology , biology
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 32 P‐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.