期刊
ONCOGENE
卷 27, 期 -, 页码 S93-S104出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/onc.2009.47
关键词
Bid; apoptosis; BH-regions; structural homology; multidomain apoptosis proteins
资金
- Canadian Institute of Health Research (CIHR) [FRN12517]
- Tier I Canada Research Chair in Membrane Biogenesis
Bid, a pro-apoptotic member of the Bcl-2 family, was initially discovered through binding to both pro-apoptotic Bax and anti-apoptotic Bcl-2. During apoptosis, Bid can be cleaved not only by caspase-8 during death receptor apoptotic signaling, but also by other caspases, granzyme B, calpains and cathepsins. Protease-cleaved Bid migrates to mitochondria where it inducespe rmeabilization of the outer mitochondrial membrane that isdependent on the pro-apoptotic proteinsBax and/or Bak, and thus Bid acts as a sentinel for protease-mediated death signals. Although sequence analysis suggests that Bid belongs to the BH3-only subgroup of the Bcl-2 family, structural and phylogenetic analysis suggests that Bid may be more related to multi-BH region proteinss such as pro-apoptotic Bax. Analysis of membrane binding by protease-cleaved Bid reveals mechanistic similarities with the membrane binding of Bax. For both proteins, membrane binding is characterized by relief of N-terminal inhibition of sequences promoting migration to membranes, insertion into the bilayer of the central hydrophobic hairpin helices and exposure of the BH3 region. These findings implicate Bid as a BH3-only protein that is both structurally and functionally related to multi-BH region Bcl-2 family proteins such as Bax. Oncogene (2009) 27, S93-S104; doi: 10.1038/onc.2009.47
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