Evidence for communication between nerve growth factor and protein tyrosine phosphorylation

Néstor Gómez; Nicholas K. Tonks; Christine Morrison; Tony Harmar; Philip Cohen

doi:10.1016/0014-5793(90)80386-W

Evidence for communication between nerve growth factor and protein tyrosine phosphorylation

Néstor Gómez, Nicholas K. Tonks, Christine Morrison, Tony Harmar, Philip Cohen

Research output: Contribution to journal › Article › peer-review

94 Citations (Scopus)

Abstract

Nerve growth factor (NGF) stimulation of PC12 cells activated two myelin basic protein (MBP) kinase activities > 10-fold within 5 min, which were resolved by chromatography on Mono Q. Each enzyme phosphorylated MBP on threonine and was inactivated by incubation with either CD45, a protein tyrosine phosphatase, or protein phosphatase 2A (PP2A), a serine/threonine phosphatase. The effects of CD45 and PP2A were prevented by vanadate and okadaic acid, respectively. Activation of the MBP-kinases provides a mechanism for communication between NGF and intracellular protein tyrosine phosphorylation.

Original language	English
Pages (from-to)	119-122
Number of pages	4
Journal	FEBS Letters
Volume	271
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(90)80386-W
Publication status	Published - 1 Oct 1990

Keywords

Nerve growth factor
Okadaic acid
PC12 cell
Protein kinase
Protein phosphatase
Tyrosine phosphorylation

ASJC Scopus subject areas

Structural Biology
Biophysics
Biochemistry
Molecular Biology
Genetics
Cell Biology

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title = "Evidence for communication between nerve growth factor and protein tyrosine phosphorylation",

abstract = "Nerve growth factor (NGF) stimulation of PC12 cells activated two myelin basic protein (MBP) kinase activities > 10-fold within 5 min, which were resolved by chromatography on Mono Q. Each enzyme phosphorylated MBP on threonine and was inactivated by incubation with either CD45, a protein tyrosine phosphatase, or protein phosphatase 2A (PP2A), a serine/threonine phosphatase. The effects of CD45 and PP2A were prevented by vanadate and okadaic acid, respectively. Activation of the MBP-kinases provides a mechanism for communication between NGF and intracellular protein tyrosine phosphorylation.",

keywords = "Nerve growth factor, Okadaic acid, PC12 cell, Protein kinase, Protein phosphatase, Tyrosine phosphorylation",

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T1 - Evidence for communication between nerve growth factor and protein tyrosine phosphorylation

AU - Gómez, Néstor

AU - Tonks, Nicholas K.

AU - Morrison, Christine

AU - Harmar, Tony

AU - Cohen, Philip

PY - 1990/10/1

Y1 - 1990/10/1

N2 - Nerve growth factor (NGF) stimulation of PC12 cells activated two myelin basic protein (MBP) kinase activities > 10-fold within 5 min, which were resolved by chromatography on Mono Q. Each enzyme phosphorylated MBP on threonine and was inactivated by incubation with either CD45, a protein tyrosine phosphatase, or protein phosphatase 2A (PP2A), a serine/threonine phosphatase. The effects of CD45 and PP2A were prevented by vanadate and okadaic acid, respectively. Activation of the MBP-kinases provides a mechanism for communication between NGF and intracellular protein tyrosine phosphorylation.

AB - Nerve growth factor (NGF) stimulation of PC12 cells activated two myelin basic protein (MBP) kinase activities > 10-fold within 5 min, which were resolved by chromatography on Mono Q. Each enzyme phosphorylated MBP on threonine and was inactivated by incubation with either CD45, a protein tyrosine phosphatase, or protein phosphatase 2A (PP2A), a serine/threonine phosphatase. The effects of CD45 and PP2A were prevented by vanadate and okadaic acid, respectively. Activation of the MBP-kinases provides a mechanism for communication between NGF and intracellular protein tyrosine phosphorylation.

KW - Nerve growth factor

KW - Okadaic acid

KW - PC12 cell

KW - Protein kinase

KW - Protein phosphatase

KW - Tyrosine phosphorylation

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AN - SCOPUS:0025153488

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JO - FEBS Letters

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ER -

Evidence for communication between nerve growth factor and protein tyrosine phosphorylation

Abstract

Keywords

ASJC Scopus subject areas

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