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 Scopus citations

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
State	Published - 14 Mar 1994
Externally published	Yes

Keywords

Amino acid sequence
Growth factor
MAP kinase
MAP kinase kinase
Phosphopeptide

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10.1016/0014-5793(94)80252-1

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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",

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

language = "English",

volume = "341",

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journal = "FEBS Letters",

issn = "0014-5793",

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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 - https://www.scopus.com/pages/publications/0028284969

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

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