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Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics.

Author information

Affiliations

  • 1. Howard Hughes Medical Institute, Department of Pathology, Harvard Medical School, Dana-Farber Cancer Institute, Boston, MA 02115, USA.
      Authors
    • Letai A 1
    (1 author)

ORCIDs linked to this article

Cancer Cell, 01 Sep 2002, 2(3):183-192
https://doi.org/10.1016/s1535-6108(02)00127-7 PMID: 12242151 

Abstract 

The "BH3-only" proteins of the BCL-2 family require "multidomain" proapoptotic members BAX and BAK to release cytochrome c from mitochondria and kill cells. We find short peptides representing the alpha-helical BH3 domains of BID or BIM are capable of inducing oligomerization of BAK and BAX to release cytochrome c. Another subset characterized by the BH3 peptides from BAD and BIK cannot directly activate BAX, BAK but instead binds antiapoptotic BCL-2, resulting in the displacement of BID-like BH3 domains that initiate mitochondrial dysfunction. Transduced BAD-like and BID-like BH3 peptides also displayed synergy in killing leukemic cells. These data support a two-class model for BH3 domains: BID-like domains that "activate" BAX, BAK and BAD-like domains that "sensitize" by occupying the pocket of antiapoptotic members.

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Read article at publisher's site: https://doi.org/10.1016/s1535-6108(02)00127-7

Read article for free, from open access legal sources, via Unpaywall: http://www.cell.com/article/S1535610802001277/pdfUnpaywall

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Funding 

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NCI NIH HHS (1)