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• W4308000147 abstract "Abstract The anti-apoptotic MCL1 is critical for delaying apoptosis during mitotic arrest. MCL1 is degraded progressively during mitotic arrest, removing its anti-apoptotic function. We found that knockout of components of ubiquitin ligases including APC/C, SCF complexes, and the mitochondrial ubiquitin ligase MARCH5 did not prevent mitotic degradation of MCL1. Nevertheless, MARCH5 determined the initial level of MCL1–NOXA network upon mitotic entry and hence the window of time during MCL1 was present during mitotic arrest. Paradoxically, although knockout of MARCH5 elevated mitotic MCL1, mitotic apoptosis was in fact enhanced in a BAK-dependent manner. Mitotic apoptosis was accelerated after MARCH5 was ablated in both the presence and absence of MCL1. Cell death was not altered after disrupting other MARCH5-regulated BCL2 family members including NOXA, BIM, and BID. Disruption of the mitochondrial fission factor DRP1, however, reduced mitotic apoptosis in MARCH5-disrupted cells. These data suggest that MARCH5 regulates mitotic apoptosis through MCL1-independent mechanisms including mitochondrial maintenance that can overcome the stabilization of MCL1." @default.
• W4308000147 created "2022-11-07" @default.
• W4308000147 creator A5003642180 @default.
• W4308000147 creator A5070555595 @default.
• W4308000147 date "2022-11-03" @default.
• W4308000147 modified "2023-10-17" @default.
• W4308000147 title "MARCH5 regulates mitotic apoptosis through MCL1-dependent and independent mechanisms" @default.
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• W4308000147 doi "https://doi.org/10.1038/s41418-022-01080-2" @default.
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