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Phosphorylation and Proteasome-Dependent Degradation of Bcl-2 in Mitotic-Arrested Cells after Microtubule Damage

Abstract : Treatment of NIH-OVCAR-3 cells with paclitaxel, a microtubule-stabilizing agent, induces mitotic arrest and apoptosis, but also Bcl-2 phosphorylation. We report here that Bcl-2 phosphorylation precedes Bcl-2 down-regulation and that both events are closely associated with mitotic arrest, but are not sufficient for paclitaxel to trigger apoptosis. Indeed, when paclitaxel-treated cells were induced to exit mitosis in the presence of 2-aminopurine, Bcl-2 phosphorylation and Bcl-2 down-regulation were both inhibited. In contrast, when apoptosis was inhibited by a caspase inhibitor or Bcl-2 over-expression, Bcl-2 phosphorylation and down-regulation still occurred. Furthermore, we show that Bcl-2 is degraded in mitosis by the proteasome-dependent pathway since Bcl-2 down-regulation is inhibited by proteasome inhibitors such as MG132, Lactacystin and LLnL. Taken together these results indicate that mitotic spindle damage results in post-translational modifications of Bcl-2 by phosphorylation and degradation.
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https://www.hal.inserm.fr/inserm-03241619
Contributor : Philippe Chadebech Connect in order to contact the contributor
Submitted on : Friday, May 28, 2021 - 5:56:59 PM
Last modification on : Wednesday, October 20, 2021 - 2:36:55 AM
Long-term archiving on: : Sunday, August 29, 2021 - 7:46:19 PM

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Philippe Chadebech, Laetitia Brichese, Véronique Baldin, Simone Vidal, Annie Valette. Phosphorylation and Proteasome-Dependent Degradation of Bcl-2 in Mitotic-Arrested Cells after Microtubule Damage. Biochemical and Biophysical Research Communications, Elsevier, 1999, 262 (3), pp.823-827. ⟨10.1006/bbrc.1999.1291⟩. ⟨inserm-03241619⟩

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