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The BCL-2 protein family: opposing activities that mediate cell death

The BCL-2 protein family: opposing activities that mediate cell death B-cell lymphoma-2 (BCL-2) family proteins regulate programmed cell death. Some members of the family (such as BCL-2 and BCL-XL) inhibit apoptosis, whereas others (such as BAX and BAK) promote cell death. BH3-only proteins are a distinct and structurally diverse class of proteins that share one motif, the BH3 domain, with BCL-2 family proteins. BH3-only proteins serve as death sentinels and transmit a signal to promote apoptosis to the core BCL-2 family proteins. Various BH3-only proteins interact with specific subsets of anti-apoptotic BCL-2 family members, yielding combinatorial signalling pathways towards apoptosis. Different tissues die prematurely in mice that lack different anti-apoptotic BCL-2 family members. Knockout of certain BH3-only proteins can compensate for the specific tissue defects that are found in mice deficient in BCL-2 family members. At the onset of apoptosis, BAX and BAK undergo conformational changes, cause the outer membrane of the mitochondria to become permeable to various proteins and induce mitochondria to fragment into smaller units. The changes in mitochondria during apoptosis, especially the release of cytochrome c, result in the activation of caspase proteases that orchestrate the efficient dismantling of dying cells. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Reviews Molecular Cell Biology Springer Journals

The BCL-2 protein family: opposing activities that mediate cell death

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References (178)

Publisher
Springer Journals
Copyright
Copyright © 2008 by Nature Publishing Group
Subject
Life Sciences; Life Sciences, general; Cell Biology; Cancer Research; Developmental Biology; Stem Cells; Biochemistry, general
ISSN
1471-0072
eISSN
1471-0080
DOI
10.1038/nrm2308
Publisher site
See Article on Publisher Site

Abstract

B-cell lymphoma-2 (BCL-2) family proteins regulate programmed cell death. Some members of the family (such as BCL-2 and BCL-XL) inhibit apoptosis, whereas others (such as BAX and BAK) promote cell death. BH3-only proteins are a distinct and structurally diverse class of proteins that share one motif, the BH3 domain, with BCL-2 family proteins. BH3-only proteins serve as death sentinels and transmit a signal to promote apoptosis to the core BCL-2 family proteins. Various BH3-only proteins interact with specific subsets of anti-apoptotic BCL-2 family members, yielding combinatorial signalling pathways towards apoptosis. Different tissues die prematurely in mice that lack different anti-apoptotic BCL-2 family members. Knockout of certain BH3-only proteins can compensate for the specific tissue defects that are found in mice deficient in BCL-2 family members. At the onset of apoptosis, BAX and BAK undergo conformational changes, cause the outer membrane of the mitochondria to become permeable to various proteins and induce mitochondria to fragment into smaller units. The changes in mitochondria during apoptosis, especially the release of cytochrome c, result in the activation of caspase proteases that orchestrate the efficient dismantling of dying cells.

Journal

Nature Reviews Molecular Cell BiologySpringer Journals

Published: Jan 1, 2008

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