Ontology highlight
ABSTRACT:
SUBMITTER: Leshchiner ES
PROVIDER: S-EPMC3600461 | biostudies-literature | 2013 Mar
REPOSITORIES: biostudies-literature
Leshchiner Elizaveta S ES Braun Craig R CR Bird Gregory H GH Walensky Loren D LD
Proceedings of the National Academy of Sciences of the United States of America 20130212 11
Proapoptotic B-cell lymphoma 2 (BCL-2) antagonist/killer (BAK) and BCL-2-associated X (BAX) form toxic mitochondrial pores in response to cellular stress. Whereas BAX resides predominantly in the cytosol, BAK is constitutively localized to the outer mitochondrial membrane. Select BCL-2 homology domain 3 (BH3) helices activate BAX directly by engaging an α1/α6 trigger site. The inability to express full-length BAK has hampered full dissection of its activation mechanism. Here, we report the produ ...[more]