Evidence for communication between nerve growth factor and protein tyrosine phosphorylation

N Gómez; N K Tonks; C Morrison; T Harmar; P Cohen

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

Evidence for communication between nerve growth factor and protein tyrosine phosphorylation

FEBS Lett. 1990 Oct 1;271(1-2):119-22. doi: 10.1016/0014-5793(90)80386-w.

Authors

N Gómez¹, N K Tonks, C Morrison, T Harmar, P Cohen

Affiliation

¹ Department of Biochemistry, University of Dundee, UK.

PMID: 2171996
DOI: 10.1016/0014-5793(90)80386-w

Abstract

Nerve growth factor (NGF) stimulation of PC12 cells activated two myelin basic protein (MBP) kinase activities greater than 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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Enzyme Activation
Nerve Growth Factors / pharmacology*
Phosphoprotein Phosphatases / metabolism*
Phosphorylation / drug effects
Protein Kinases / metabolism*
Protein Phosphatase 2
Protein Serine-Threonine Kinases
Protein Tyrosine Phosphatases
Rats
Tumor Cells, Cultured

Substances

Nerve Growth Factors
Protein Kinases
Protein Serine-Threonine Kinases
Phosphoprotein Phosphatases
Protein Phosphatase 2
Protein Tyrosine Phosphatases