Reversible Tyrosine Phosphorylation of Cdc2 - Dephosphorylation Accompanies Activation During Entry into Mitosis

Morla, A. O., Draetta, G., Beach, D., Wang, J. Y. J. (1989) Reversible Tyrosine Phosphorylation of Cdc2 - Dephosphorylation Accompanies Activation During Entry into Mitosis. Cell, 58 (1). pp. 193-203. ISSN 0092-8674

URL: http://www.ncbi.nlm.nih.gov/pubmed/2473839
DOI: 10.1016/0092-8674(89)90415-7

Abstract

Tyrosine phosphorylation of cdc2 is regulated in the cell cycle of mouse 3T3 fibroblasts. Phosphotyrosine in cdc2 is detectable at the onset of DNA synthesis and becomes maximal in the G2 phase of the cell cycle. Quantitative tyrosine dephosphorylation of cdc2 occurs during entry into mitosis and no phosphotyrosine is detected during the G1 phase of the cell cycle. While increasing tyrosine phosphorylation of cdc2 correlates with the formation of a cdc2/p62 complex, the tyrosine phosphorylated cdc2 is inactive as a histone H1 kinase. cdc2 is fully dephosphorylated in its most active mitotic form, yet specific tyrosine dephosphorylation of interphase cdc2 in vitro is insufficient to activate the kinase. In vivo inhibition of tyrosine dephosphorylation by exposure of cells to a phosphatase inhibitor is associated with G2 arrest, which is reversible upon the removal of the phosphatase inhibitor. Tyrosine dephosphorylation of cdc2 may be one of a number of obligatory steps in the mitotic activation of the kinase.

Item Type: Paper
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > cdc2
organs, tissues, organelles, cell types and functions > organelles, types and functions > mitosis
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase > tyrosine kinase
CSHL Authors:
Communities: CSHL labs > Beach lab
Depositing User: Gail Sherman
Date: 14 July 1989
Date Deposited: 28 Jun 2017 15:21
Last Modified: 28 Jun 2017 15:21
Related URLs:
URI: http://repository.cshl.edu/id/eprint/34886

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