Portal de investigación
Bax transmembrane domain interacts with prosurvival Bcl-2 proteins in biological membranes
Fecha de publicación:
Autores de CIPF
Participantes ajenos a CIPF
- Andreu-Fernandez, V
- Genoves, A
- Todt, F
- Lauterwasser, J
- Funk, K
- Jahreis, G
- Mingarro, I
- Edlich, F
Grupos de Investigación
Abstract
The Bcl-2 (B-cell lymphoma 2) protein Bax (Bcl-2 associated X, apoptosis regulator) can commit cells to apoptosis via outer mitochondrial membrane permeabilization. Bax activity is controlled in healthy cells by prosurvival Bcl-2 proteins. C-terminal Bax transmembrane domain interactions were implicated recently in Bax pore formation. Here, we show that the isolated transmembrane domains of Bax, Bcl-xL (B-cell lymphoma-extra large), and Bcl-2 can mediate interactions between Bax and prosurvival proteins inside the membrane in the absence of apoptotic stimuli. Bcl-2 protein transmembrane domains specifically homooligomerize and heterooligomerize in bacterial and mitochondrial membranes. Their interactions participate in the regulation of Bcl-2 proteins, thus modulating apoptotic activity. Our results suggest that interactions between the transmembrane domains of Bax and antiapoptotic Bcl-2 proteins represent a previously unappreciated level of apoptosis regulation.
Datos de la publicación
- ISSN/ISSNe:
- 0027-8424, 1091-6490
- Tipo:
- Article
- Páginas:
- 310-315
- PubMed:
- 28028215
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA NATL ACAD SCIENCES
Citas Recibidas en Web of Science: 81
Documentos
- No hay documentos
Filiaciones
Keywords
- apoptosis; Bcl-2; mitochondria; oligomerization; transmembrane
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