NDLI: Modulation of cell death by $Bcl-x_{L}$ through caspase interaction

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Modulation of cell death by $Bcl-x_{L}$ through caspase interaction

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Cheng, E. H. Takahashi, A. Hardwick, J. M. Kirsch, D. G. Kastan, M. B. Griffin, D. E. Ueno, K. Karp, C. L. Earnshaw, W. C. Clem, R. J. Veliuona, M. A.
Description	Author Affiliation: Clem RJ ( Department of Molecular Microbiology and Immunology, Johns Hopkins University Schools of Public Health and Medicine, Baltimore, MD 21205, USA.);
Abstract	The caspases are cysteine proteases that have been implicated in the execution of programmed cell death in organisms ranging from nematodes to humans. Many members of the Bcl-2 family, including Bcl-XL, are potent inhibitors of programmed cell death and inhibit activation of caspases in cells. Here, we report a direct interaction between caspases and Bcl-XL. The loop domain of Bcl-XL is cleaved by caspases in vitro and in cells induced to undergo apoptotic death after Sindbis virus infection or interleukin 3 withdrawal. Mutation of the caspase cleavage site in Bcl-XL in conjunction with a mutation in the BH1 homology domain impairs the death-inhibitory activity of Bcl-XL, suggesting that interaction of Bcl-XL with caspases may be an important mechanism of inhibiting cell death. However, once Bcl-XL is cleaved, the C-terminal fragment of Bcl-XL potently induces apoptosis. Taken together, these findings indicate that the recognition/cleavage site of Bcl-XL may facilitate protection against cell death by acting at the level of caspase activation and that cleavage of Bcl-XL during the execution phase of cell death converts Bcl-XL from a protective to a lethal protein.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	2
Volume Number	95
Language	English
Publisher	National Academy of Sciences
Publisher Date	1998-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Apoptosis Cysteine Endopeptidases Physiology Proto-Oncogene Proteins C-bcl-2 Signal Transduction Cell Line Enzyme Activation Escherichia Coli Mutation Bcl-X Protein Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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