The phosphorylation of stathmin by MAP kinase
- 1 November 1993
- journal article
- protein phosphorylation-in-signal-transduction
- Published by Springer Nature in Molecular and Cellular Biochemistry
- Vol. 127-128 (1) , 151-156
- https://doi.org/10.1007/bf01076766
Abstract
Stathmin, a ubiquitous cytosolic phosphoprotei which may play a role in integrating the effects of diverse signals regulating proliferation, differentiation and other cell functions, was found to be phosphorylated rapidly and stoichiometrically by mitogen-activated protein (MAP) kinasein vitro. Ser-25 was identified as the major site and Ser-38 as a minor site of phosphorylation, while the p42 and p44 isoforms of MAP kinase were the only significant stathmin kinases detected in PC12 cells after stimulation by nerve growth factor (NGF). The results suggest that MAP kinases are the enzymes responsible for increasing the level of phosphorylation of Ser-25, which has been observed previously in PC12 cells following stimulation by NGF.Keywords
This publication has 35 references indexed in Scilit:
- High expression of stathmin in multipotential teratocarcinoma and normal embryonic cells versus their early differentiated derivativesDifferentiation, 1992
- Stathmin Phosphorylation Is Regulated in Striatal Neurons by Vasoactive Intestinal Peptide and Monoamines via Multiple Intracellular PathwaysJournal of Neurochemistry, 1992
- Differential mRNA expression of the phosphoprotein p19/SCG10 gene family in mouse preimplantation embryos, uterus, and placentaReproduction, Fertility and Development, 1992
- Dissection of the protein kinase cascade by which nerve growth factor activates MAP kinasesNature, 1991
- Stathmin phosphorylation patterns discriminate between distinct transduction pathways of human T lymphocyte activation through CD2 triggeringFEBS Letters, 1991
- ERKs: A family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGFCell, 1991
- Evidence for communication between nerve growth factor and protein tyrosine phosphorylationFEBS Letters, 1990
- A single amino acid difference distinguishes the human and the rat sequences of stathmin, a ubiquitous intracellular phosphoprotein associated with cell regulationsFEBS Letters, 1990
- Stathmin Is a Major Phosphoprotein and Cyclic AMP‐Dependent Protein Kinase Substrate in Mouse Brain Neurons but Not in Astrocytes in Culture: Regulation During OntogenesisJournal of Neurochemistry, 1989
- Protein phosphorylation in response to the tumor promoter TPA is dependent on the state of differentiation of muscle cellsDevelopmental Biology, 1987