BAX unleashed: The biochemical transformation of an inactive cytosolic monomer into a toxic mitochondrial pore

Loren D. Walensky, Evripidis Gavathiotis

Research output: Contribution to journalReview articlepeer-review

119 Scopus citations

Abstract

BAX, the BCL-2-associated X protein, is a cardinal proapoptotic member of the BCL-2 family, which regulates the critical balance between cellular life and death. Because so many medical conditions can be categorized as diseases of either too many or too few cells, dissecting the biochemistry of BCL-2 family proteins and developing pharmacological strategies to target them have become high priority scientific objectives. Here, we focus on BAX, a latent, cytosolic and monomeric protein that transforms into a lethal mitochondrial oligomer in response to cellular stress. New insights into the structural location of BAX's 'on switch', and the multi-step conformational changes that ensue upon BAX activation, are providing fresh opportunities to modulate BAX for potential benefit in human diseases characterized by pathologic cell survival or unwanted cellular demise.

Original languageEnglish (US)
Pages (from-to)642-652
Number of pages11
JournalTrends in Biochemical Sciences
Volume36
Issue number12
DOIs
StatePublished - Dec 1 2011

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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