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Science 13 April 1990:
Vol. 248. no. 4952, pp. 217 - 220
DOI: 10.1126/science.2183353
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Articles

Science, Vol 248, Issue 4952, 217-220
Copyright © 1990 by American Association for the Advancement of Science

articles

Differential phosphorylation of c-Abl in cell cycle determined by cdc2 kinase and phosphatase activity

ET Kipreos and JY Wang

Department of Biology, University of California, San Diego, La Jolla 92093.

The product of the c-abl proto-oncogene (c-Abl) is phosphorylated on three sites during interphase and seven additional sites during mitosis. Two interphase and all mitotic c-Abl sites are phosphorylated by cdc2 kinase isolated from either interphase or mitotic cells, with the mitotic cdc2 having an 11-fold higher activity. Inhibition of phosphatases with okadaic acid in interphase cells leads to the phosphorylation of c-Abl mitotic sites, indicating that those sites are preferentially dephosphorylated during interphase. The differential phosphorylation of c-Abl in the cell cycle is therefore determined by an equilibrium between cdc2 kinase and protein phosphatase activities. Treatment of interphase cells with okadaic acid leads to a rounded morphology similar to that observed during mitosis.


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