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

doi:10.1016/0014-5793(94)80252-1

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 journal › Article › peer-review

38 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 language	English
Pages (from-to)	119-124
Number of pages	6
Journal	FEBS Letters
Volume	341
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(94)80252-1
Publication status	Published - 14 Mar 1994

Keywords

Amino acid sequence
Growth factor
MAP kinase
MAP kinase kinase
Phosphopeptide

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/0014-5793(94)80252-1Licence: No Licence / Unknown

Cite this

@article{a5081d7f51634638b12d13d226bd992e,

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.",

keywords = "Amino acid sequence, Growth factor, MAP kinase, MAP kinase kinase, Phosphopeptide",

author = "Yuji Saito and Nestor Gomez and Campbell, {David G.} and Alan Ashworth and Marshall, {Chris J.} and Philip Cohen",

year = "1994",

month = mar,

day = "14",

doi = "10.1016/0014-5793(94)80252-1",

language = "English",

volume = "341",

pages = "119--124",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Wiley",

number = "1",

}

TY - JOUR

T1 - 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

AU - Saito, Yuji

AU - Gomez, Nestor

AU - Campbell, David G.

AU - Ashworth, Alan

AU - Marshall, Chris J.

AU - Cohen, Philip

PY - 1994/3/14

Y1 - 1994/3/14

N2 - 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.

AB - 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.

KW - Amino acid sequence

KW - Growth factor

KW - MAP kinase

KW - MAP kinase kinase

KW - Phosphopeptide

UR - http://www.scopus.com/inward/record.url?scp=0028284969&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(94)80252-1

DO - 10.1016/0014-5793(94)80252-1

M3 - Article

C2 - 8137910

AN - SCOPUS:0028284969

SN - 0014-5793

VL - 341

SP - 119

EP - 124

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

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

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this