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.

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Saito Y,Gomez N,Campbell DG,Ashworth A,Marshall CJ,Cohen P

doi

10.1016/0014-5793(94)80252-1

subject

Has Abstract

pub_date

1994-03-14 00:00:00

pages

119-24

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(94)80252-1

journal_volume

341

pub_type

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