Journal
TRENDS IN CELL BIOLOGY
Volume 18, Issue 4, Pages 157-164Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tcb.2008.01.007
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Funding
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI040646] Funding Source: NIH RePORTER
- NIAID NIH HHS [R01 AI040646, R01 AI040646-14] Funding Source: Medline
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The mitochondrial pathway of apoptosis proceeds when molecules sequestered between the outer and inner mitochondrial membranes are released to the cytosol by mitochondrial outer membrane permeabilization (MOMP). This process is controlled by the BCL-2 family, which is composed of both pro- and anti-apoptotic proteins. Although there is no disagreement that BCL-2 proteins regulate apoptosis, the mechanism leading to MOMP remains controversial. Current debate focuses on what interactions within the family are crucial to initiate MOMP. Specifically, do the BH3-only proteins directly engage BAX and/or BAK activation or do these proteins solely promote apoptosis by neutralization of anti-apoptotic BCL-2 proteins? We describe these models and contend that BH3-only proteins must perform both functions to efficiently engage MOMP and apoptosis.
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