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Bid Induces the Oligomerization and Insertion of Bax into the Outer Mitochondrial Membrane

Molecular and Cellular Biology · 2000 · Vol. 20(3) · pp. 929–935

Abstract

In many types of apoptosis, the proapoptotic protein Bax undergoes a change in conformation at the level of the mitochondria. This event always precedes the release of mitochondrial cytochrome c, which, in the cytosol, activates caspases through binding to Apaf-1. The mechanisms by which Bax triggers cytochrome c release are unknown. Here we show that following binding to the BH3-domain-only proapoptotic protein Bid, Bax oligomerizes and then integrates in the outer mitochondrial membrane, where it triggers cytochrome c release. Bax mitochondrial membrane insertion triggered by Bid may represent a key step in pathways leading to apoptosis.

Cell death mechanisms and regulationCytochrome cBiologyMitochondrionCytosolMitochondrial apoptosis-induced channelCell biologyBacterial outer membraneCaspaseApoptosisInner mitochondrial membrane

MeSH terms

Carrier ProteinsCytochrome c GroupDigitoninHeLa CellsHumansIntracellular MembranesMitochondriaModels, BiologicalProto-Oncogene ProteinsSignal TransductionApoptosisProto-Oncogene Proteins c-bcl-2Genes, bcl-2StaurosporineProtein Structure, Quaternary
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