Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax.
Cell
; 135(6): 1074-84, 2008 Dec 12.
Article
em En
| MEDLINE
| ID: mdl-19062087
In normal circumstances, the Bcl-2 family dutifully governs when cells die. However, the rules of engagement between the pro- and antiapoptotic family members are still contested, and how Bax is transformed from a cytosolic monomer to an outer mitochondrial membrane-permeabilizing oligomer is unclear. With fluorescence techniques and an in vitro system, the combination of tBid and Bax produced dramatic membrane permeabilization. The membrane is not a passive partner in this process beause membranes are required for the protein-protein interactions to occur. Simultaneous measurements of these interactions revealed an ordered series of steps required for outer membrane permeabilization: (1) tBid rapidly binds to membranes, where (2) tBid interacts with Bax, causing (3) Bax insertion into membranes and (4) oligomerization, culminating in (5) membrane permeabilization. Bcl-XL prevents membrane-bound tBid from binding Bax. Bad releases tBid from Bcl-XL, restoring both tBid binding to Bax and membrane permeabilization.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Apoptose
/
Membranas Mitocondriais
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Proteína X Associada a bcl-2
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Proteína Agonista de Morte Celular de Domínio Interatuante com BH3
Limite:
Animals
Idioma:
En
Revista:
Cell
Ano de publicação:
2008
Tipo de documento:
Article
País de afiliação:
Canadá