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

Evidence for communication between nerve growth factor and protein tyrosine phosphorylation

N Gómez  1 , N K Tonks, C Morrison, T Harmar, P Cohen
Affiliations
Free article

Evidence for communication between nerve growth factor and protein tyrosine phosphorylation

N Gómez et al. FEBS Lett. .
Free article

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.

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