title: 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.
authors.affiliation: Department of Biochemistry, University of Dundee, UK.
authors.forename: Y
authors.initials: Y
authors.lastname: Saito
authors.forename: N
authors.initials: N
authors.lastname: Gomez
authors.forename: D G
authors.initials: DG
authors.lastname: Campbell
authors.forename: A
authors.initials: A
authors.lastname: Ashworth
authors.forename: C J
authors.initials: CJ
authors.lastname: Marshall
authors.forename: P
authors.initials: P
authors.lastname: Cohen
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D048369:MAP Kinase Kinase 1; D051379:Mice; D019950:Mitogen-Activated Protein Kinase 1; D020929:Mitogen-Activated Protein Kinase Kinases; D008969:Molecular Sequence Data; D009414:Nerve Growth Factors / Q000494:pharmacology*; D016716:PC12 Cells; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D011817:Rabbits; D051381:Rats; D013912:Threonine / Q000378:metabolism*
chemical_list: D009414:Nerve Growth Factors; D013912:Threonine; D011505:Protein-Tyrosine Kinases; D017346:Protein Serine-Threonine Kinases; D019950:Mitogen-Activated Protein Kinase 1; D048369:MAP Kinase Kinase 1; C482127:Map2k1 protein, mouse; D020929:Mitogen-Activated Protein Kinase Kinases