Journal
CELLULAR SIGNALLING
Volume 23, Issue 12, Pages 2030-2038Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.cellsig.2011.07.017
Keywords
Bcl-xL; PLK3; Cell cycle; G2 arrest; Cytokinesis; Mitotic exit
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Funding
- Canadian Institutes of Health Research [MOP-97913]
- China Scholarship Council (Beijing, China)
- Faculte des etudes superieures (Universite de Montreal, Canada)
- Fondation de l'Institut du cancer de Montreal (Canada)
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Functional analysis of a Bcl-xL phosphorylation mutant series has revealed that cells expressing Bcl-xL(Ser49Ala) mutant are less stable at G2 checkpoint after DNA damage and enter cytokinesis more slowly after microtubule poisoning, than cells expressing wild-type Bcl-xl.. These effects of Bcl-xL(Ser49Ala) mutant seem to be separable from Bcl-xL function in apoptosis. Bcl-xL(Ser49) phosphorylation is cell cycle-dependent. In synchronized cells, phospho-Bcl-xL(Ser49) appears during the S phase and G2, whereas it disappears rapidly in early mitosis during prometaphase, metaphase and early anaphase, and re-appears during telophase and cytokinesis. During DNA damage-induced G2 arrest, an important pool of phospho-Bcl-xL(Ser49) accumulates in centrosomes which act as essential decision centers for progression from G2 to mitosis. During telophase/cytokinesis, phospho-Bcl-xL (Ser49) is found with dynein motor protein. In a series of in vitro kinase assays, specific small interfering RNA and pharmacological inhibition experiments, polo kinase 3 (PLK3) was implicated in Bcl-xL(Ser49) phosphorylation. These data indicate that, during G2 checkpoint, phospho-Bcl-xL(Ser49) is another downstream target of PLK3, acting to stabilize G2 arrest. Bcl-xL phosphorylation at Ser49 also correlates with essential PLK3 activity and function, enabling cytokinesis and mitotic exit. (C) 2011 Elsevier Inc. All rights reserved.
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