The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Modulation of cell death by Bcl-x L through caspase interaction
Open accessAbstract
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-x L , are potent inhibitors of programmed cell death and inhibit activation of caspases in cells. Here, we report a direct interaction between caspases and Bcl-x L . The loop domain of Bcl-x L 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-x L in conjunction with a mutation in the BH1 homology domain impairs the death-inhibitory activity of Bcl-x L , suggesting that interaction of Bcl-x L with caspases may be an important mechanism of inhibiting cell death. However, once Bcl-x L is cleaved, the C-terminal fragment of Bcl-x L potently induces apoptosis. Taken together, these findings indicate that the recognition/cleavage site of Bcl-x L may facilitate protection against cell death by acting at the level of caspase activation and that cleavage of Bcl-x L during the execution phase of cell death converts Bcl-x L from a protective to a lethal protein.
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Citations
Cites
Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programed cell death
Oltval, Z. N., Milliman, C. L., & Korsmeyer, S. J. (1993) · Cell · doi:10.1016/0092-8674(93)90509-o · Cited by 6,003
Cited by
Cleavage of BID by Caspase 8 Mediates the Mitochondrial Damage in the Fas Pathway of Apoptosis
Li, H., Zhu, H., Xu, C.-J., & Yuan, J. (1998) · Cell · doi:10.1016/s0092-8674(00)81590-1 · Cited by 4,445
Mammalian Caspases: Structure, Activation, Substrates, and Functions During Apoptosis
Earnshaw, W. C., Martins, L. M., & Kaufmann, S. H. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.383 · Cited by 2,760
Self-citationNF-κB at the crossroads of life and death
Karin, M., & Lin, A. (2002) · Nature Immunology · doi:10.1038/ni0302-221 · Cited by 2,709
Intrinsically disordered protein
Dunker, A. K., Lawson, J. D., Brown, C. J., Williams, R. M., Romero, P., Oh, J. S., Oldfield, C. J., Campen, A. M., Ratliff, C. M., Hipps, K. W., et al. (2001) · Journal of Molecular Graphics and Modelling · doi:10.1016/s1093-3263(00)00138-8 · Cited by 2,272
Intrinsically Disordered Proteins
Uversky, V. N. (2013) · Brenner's Encyclopedia of Genetics · doi:10.1016/b978-0-12-374984-0.01698-3 · Cited by 1,637
Metadata
- Authors
- Clem, R. J., Cheng, E. H.-Y., Karp, C. L., Kirsch, D. G., Ueno, K., Takahashi, A., Kastan, M. B., Griffin, D. E., Earnshaw, W. C., Veliuona, M. A., & Hardwick, J. M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1998-01-20
- Volume
- 95
- Issue
- 2
- Pages
- 554-559
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2098160574
- Cited by
- 514
- References
- 1
- FWCI
- 19.36
- Type
- journal article
- Language
- en
- Open access
- green
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- Clem, R. J., Cheng, E. H.-Y., Karp, C. L., Kirsch, D. G., Ueno, K., Takahashi, A., Kastan, M. B., Griffin, D. E., Earnshaw, W. C., Veliuona, M. A., & Hardwick, J. M. (1998). Modulation of cell death by Bcl-x L through caspase interaction. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.95.2.554
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