Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane
R Eskes, S Desagher, B Antonsson… - Molecular and cellular …, 2000 - Am Soc Microbiol
R Eskes, S Desagher, B Antonsson, JC Martinou
Molecular and cellular biology, 2000•Am Soc MicrobiolIn 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 …
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 …
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 cytochromec release. Bax mitochondrial membrane insertion triggered by Bid may represent a key step in pathways leading to apoptosis.
American Society for Microbiology