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

Article Details

Citation

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Tyrosine-protein kinase ABL1P00519Details