NDLI: A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax

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A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax

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A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	George, Nicholas M. Evans, Jacquelynn J. D. Luo, Xu
Description	Country affiliation: United States Author Affiliation: George NM ( Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska 68198, USA.)
Abstract	Homo-oligomerization of Bax (or Bak) has been hypothesized to be responsible for cell death through the mitochondria-dependent apoptosis pathway. However, partly due to a lack of structural information on the Bax homo-oligomerization and apoptosis inducing domain(s), this hypothesis has remained difficult to test. In this study, we identified a three-helix unit, comprised of the BH3 (helix 2) and BH1 domains (helix 4 and helix 5), as the homo-oligomerization domain of Bax. When targeted to mitochondria, this minimum oligomerization unit induced apoptosis in Bax(-/-)Bak(-/-) mouse embryonic fibroblasts (DKO). Strikingly, the central helix of Bax (helix 5), when replacing the corresponding helix (helix 5) of Bcl-xL, an anti-apoptotic Bcl-2 family protein structurally homologous to Bax, converted Bcl-xL into a Bax-like molecule capable of forming oligomers and causing apoptosis in the DKO cells. Finally, a series of systematic mutagenesis analyses revealed that homo-oligomerization is both necessary and sufficient for the apoptotic activity of Bax. These results suggest that active Bax causes mitochondrial damage through homo-oligomers of a three-helix functional unit.
File Format	HTM / HTML
ISSN	08909369
e-ISSN	15495477
Journal	Genes & Development
Issue Number	15
Volume Number	21
Language	English
Publisher	Cold Spring Harbor Laboratory Press
Publisher Date	2007-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Molecular Discipline Biology__semicolon__developmental Discipline Biology__semicolon__genetics__semicolon__cell Discipline Biology Apoptosis Physiology Bcl-2-associated X Protein Chemistry Animals Cells, Cultured Fibroblasts Cytology Metabolism Mice Mice, Knockout Models, Molecular Mutation Protein Structure, Quaternary Protein Structure, Secondary Protein Structure, Tertiary Recombinant Fusion Proteins Genetics Transfection Bcl-2 Homologous Antagonist-killer Protein Deficiency Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Genetics Developmental Biology

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A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax

Assembly of the Bak Apoptotic Pore: A CRITICAL ROLE FOR THE BAK PROTEIN α6 HELIX IN THE MULTIMERIZATION OF HOMODIMERS DURING APOPTOSIS

Active Bax and Bak are functional holins.

BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak.

Bid chimeras indicate that most BH3-only proteins can directly activate Bak and Bax, and show no preference for Bak versus Bax

DRP1-dependent apoptotic mitochondrial fission occurs independently of BAX, BAK and APAF1 to amplify cell death by BID and oxidative stress☆

tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c

In non-transformed cells Bak activates upon loss of anti-apoptotic Bcl-XL and Mcl-1 but in the absence of active BH3-only proteins.

Bid binding to negatively charged phospholipids may not be required for its pro-apoptotic activity in vivo.

A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax

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A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax

Assembly of the Bak Apoptotic Pore: A CRITICAL ROLE FOR THE BAK PROTEIN α6 HELIX IN THE MULTIMERIZATION OF HOMODIMERS DURING APOPTOSIS

Active Bax and Bak are functional holins.

BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak.

Bid chimeras indicate that most BH3-only proteins can directly activate Bak and Bax, and show no preference for Bak versus Bax

DRP1-dependent apoptotic mitochondrial fission occurs independently of BAX, BAK and APAF1 to amplify cell death by BID and oxidative stress☆

tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c

In non-transformed cells Bak activates upon loss of anti-apoptotic Bcl-XL and Mcl-1 but in the absence of active BH3-only proteins.

Bid binding to negatively charged phospholipids may not be required for its pro-apoptotic activity in vivo.

A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax