Conformation of the Bax C‐terminus regulates subcellular location and cell death

Conformation of the Bax C‐terminus regulates subcellular location and cell death Bax, a pro‐apoptotic member of the Bcl‐2 family, translocates from the cytosol to the mitochondria during programmed cell death. We report here that both gain‐of‐function and loss‐of‐function mutations can be achieved by altering a single amino acid in the Bax hydrophobic C‐terminus. The properly mutated C‐terminus of Bax can target a non‐relevant protein to the mitochondria, showing that specific conformations of this domain alone allow mitochondrial docking. These data along with N‐terminus epitope exposure experiments suggest that the C‐ and the N‐termini interact and that upon triggering of apoptosis, Bax changes conformation, exposing these two domains to insert into the mitochondria and regulate the cell death machinery. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The EMBO Journal Wiley

Conformation of the Bax C‐terminus regulates subcellular location and cell death

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Publisher
Wiley
Copyright
Copyright © 2013 Wiley Periodicals, Inc
ISSN
0261-4189
eISSN
1460-2075
DOI
10.1093/emboj/18.9.2330
Publisher site
See Article on Publisher Site

Abstract

Bax, a pro‐apoptotic member of the Bcl‐2 family, translocates from the cytosol to the mitochondria during programmed cell death. We report here that both gain‐of‐function and loss‐of‐function mutations can be achieved by altering a single amino acid in the Bax hydrophobic C‐terminus. The properly mutated C‐terminus of Bax can target a non‐relevant protein to the mitochondria, showing that specific conformations of this domain alone allow mitochondrial docking. These data along with N‐terminus epitope exposure experiments suggest that the C‐ and the N‐termini interact and that upon triggering of apoptosis, Bax changes conformation, exposing these two domains to insert into the mitochondria and regulate the cell death machinery.

Journal

The EMBO JournalWiley

Published: Apr 4, 1999

Keywords: ; ; ; ;

References

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