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Updated: Jun 18, 2026

Examining BCL-2 Family Function with Large Unilamellar Vesicles
Published on: October 5, 2012
Mcl-1(128-350) fragment induces apoptosis through direct interaction with Bax
Emmanuelle Ménoret1, Patricia Gomez-Bougie, Sylvanie Surget
1INSERM, UMR892, CRCNA, Institut de Recherche thérapeutique de l'Université de Nantes, 44007 Nantes Cedex1, France.
Abstract:
Mcl-1 full-length (Mcl-1(1-350)), a tightly regulated protein, plays an important role in protecting cells against apoptosis. Cleavage of Mcl-1 at Asp127 by caspase (Mcl-1(C1)) contributes to the regulation of Mcl-1 expression, but its pro-apoptotic function remains controversial. Here, we reported that Mcl-1(128-350) expression induced caspase-dependent apoptosis. We demonstrated that Mcl-1(128-350) but not Mcl-1(1-350) interacts with Bax. This interaction required an intact BH3 Mcl-1(128-350) domain and leads to Bax activation and translocation to mitochondria. The silencing of Bax, but not of Bak, prevented Mcl-1(128-350) induced apoptosis. In conclusion, Mcl-1(128-350) exerts a pro-apoptotic function governed by its capacity to interact with Bax.
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