Differential phosphorylation of c-Abl in cell cycle determined by cdc2 kinase and phosphatase activity.
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Kipreos ET, Wang JY
Differential phosphorylation of c-Abl in cell cycle determined by cdc2 kinase and phosphatase activity.
Science. 1990 Apr 13;248(4952):217-20.
- PubMed ID
- 2183353 [ View in PubMed]
- Abstract
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.