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- Publisher
- Annual Reviews
- Copyright
- Copyright © 1998 by Annual Reviews. All rights reserved
- Subject
- Review Articles
- ISSN
- 0732-0582
- eISSN
- 1545-3278
- DOI
- 10.1146/annurev.immunol.16.1.395
- pmid
- 9597135
- Publisher site
- See Article on Publisher Site
Abstract
▪ Abstract An expanding family of BCL-2 related proteins share homology, clustered within four conserved regions, namely BCL-2 homology (BH1-4) domains, which control the ability of these proteins to dimerize and function as regulators of apoptosis. Moreover, BCL-X L , BCL-2, and BAX can form ion-conductive pores in artificial membranes. The BCL-2 family, comprised of both pro-apoptotic and anti-apoptotic members, acts as a checkpoint upstream of CASPASES and mitochondrial dysfunction. BID and BAD possess the minimal death domain BH3, and the phosphorylation of BAD connects proximal survival signals to the BCL-2 family. BCL-2 and BCL-X L display a reciprocal pattern of expression during lymphocyte development. Gain- and loss-of-function models revealed stage-specific roles for BCL-2 and BCL-X L . BCL-2 can rescue maturation at several points of lymphocyte development. The BCL-2 family also reveals evidence for a cell-autonomous coordination between the opposing pathways of proliferation and cell death.
Journal
Annual Review of Immunology – Annual Reviews
Published: Apr 1, 1998