Bcl-2 family proteins are known to control cell death and influence mitochondrial function. The function of Mcl-1, an anti-apoptotic Bcl-2 protein, is now shown to depend on its subcellular localization. Mcl-1 at the mitochondrial outer membrane inhibits mitochondrial permeabilization to block apoptosis. However, a cleaved form of Mcl-1 localizes to the mitochondrial matrix and controls inner mitochondrial morphology and oxidative phosphorylation, without directly modulating apoptosis.
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The authors declare no competing financial interests.
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Andersen, J., Kornbluth, S. Mcl-1 rescues a glitch in the matrix. Nat Cell Biol 14, 563–565 (2012). https://doi.org/10.1038/ncb2511
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