Evidence for communication between nerve growth factor and protein tyrosine phosphorylation.
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.
Gómez
N
N
Department of Biochemistry, University of Dundee, UK.
Tonks
N K
NK
Morrison
C
C
Harmar
T
T
Cohen
P
P
D000818:Animals; D004789:Enzyme Activation; D009414:Nerve Growth Factors / Q000494:pharmacology*; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D010766:Phosphorylation / Q000187:drug effects; D011494:Protein Kinases / Q000378:metabolism*; D054648:Protein Phosphatase 2; D017346:Protein Serine-Threonine Kinases; D017027:Protein Tyrosine Phosphatases; D051381:Rats; D014407:Tumor Cells, Cultured
D009414:Nerve Growth Factors; D011494:Protein Kinases; D017346:Protein Serine-Threonine Kinases; D010749:Phosphoprotein Phosphatases; D054648:Protein Phosphatase 2; D017027:Protein Tyrosine Phosphatases