Bax-independent inhibition of apoptosis by Bcl-XL

Emily H Y Cheng, Beth Levine, Lawrence H. Boise, Craig B. Thompson, J. Marie Hardwick

Research output: Contribution to journalArticle

436 Scopus citations

Abstract

THE Bcl-2-related protein, Bcl-xL, has been shown to block apoptosis induced by a variety of stimuli1-5 and to be a stronger protector against apoptosis than BcL-2 under certain circumstances2,5. Using site-specific mutagenesis, we show here that the amino-acid residues critical for protection of cells by Bcl-xL, against Sindbis virus-induced apoptosis are clustered within the Bcl-2-homology regions 1 and 2 (BH1 and BH2 regions). The residues necessary for Bcl-xL function are not identical to those required for Bcl-2 function6. Although it has been suggested that heterodimerization between Bcl-xL and Bax is essential for the anti-death activity of Bcl-xL (refs 7,8), our results suggest that the interaction with Bax is not required for Bcl-xL to exert its death-repressing activity. Specific mutations that disrupt the ability of Bcl-xL to interact with Bax or Bax still preserve 70-80% of the anti-death activity of wild-type Bcl-xL.

Original languageEnglish (US)
Pages (from-to)554-556
Number of pages3
JournalNature
Volume379
Issue number6565
DOIs
StatePublished - Feb 8 1996

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Bax-independent inhibition of apoptosis by Bcl-X<sub>L</sub>'. Together they form a unique fingerprint.

  • Cite this

    Cheng, E. H. Y., Levine, B., Boise, L. H., Thompson, C. B., & Hardwick, J. M. (1996). Bax-independent inhibition of apoptosis by Bcl-XL. Nature, 379(6565), 554-556. https://doi.org/10.1038/379554a0