VDAC2 Inhibits BAK Activation and Mitochondrial Apoptosis

By E. Cheng, T. Sheiko, J. Fisher, W. Craigen, S. Korsmeyer. Science, 2003

854 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/31d98ba4dae18de508845e2b2f4d0c9b07452ff5

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. Douglas R. Green
2. Jerry M. Adams
3. Guido Kroemer
4. L. Galluzzi
5. Suzanne Cory
6. R. Youle
7. A. Letai
8. J. Chipuk

Citations in the corpus

• Mitochondria and cell death: outer membrane permeabilization and beyond (2010, background): “Other studies have found that VDAC2 interactions with BAK are required to hold BAK inactive or for its mitochondrial localizatio”
• Hexokinase II: Cancer's double-edged sword acting as both facilitator and gatekeeper of malignancy when bound to mitochondria (2006, background): “Opening of the MPTP by activated Bax or Bak has been variously described in the literature as due to either oligomerization of these factors within the mitochondrial membranes, or due to their interactions with VDAC-1 or VDAC-2, respectively (Cheng et al., 2003; Granville and Gottlieb, 2003).”
• Ways of dying: multiple pathways to apoptosis. (2003, background): “Similarly, in healthy but not in apoptotic cells, a small proportion of Bak molecules are bound to VDAC2, which forms a pore in the mitochondrial outer membrane (Cheng et al. 2003).”
• Mechanisms of cytochrome c release from mitochondria (2006, background): “maintained in a monomeric inactive conformation thanks to interactions with VDAC2, a scarcely expressed VDAC isoform.(59) BIM and BID are able to activate BAX in a direct fashion.”
• Mitochondrial p53 activates Bak and causes disruption of a Bak–Mcl1 complex (2004, background): “Existing data suggest that these three segments of Bak most probably form a binding pocket that would be disrupted by mutations within any one of the domain”
• Control of mitochondrial apoptosis by the Bcl-2 family (2009, background): “However, it might be that Bax and Bak can alternatively interact with proteins that remove the requirement for sequestration by anti-apoptotic proteins ( Cheng et al., 2003 ).”
• Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels (2006, background): “, 2004), and both VDAC1 and VDAC2 take part in metabolic and apoptotic protein complexes (Cheng et al., 2003; Colombini, 2004; Lemasters and Holmuhamedov, 2006).”
• Mitochondria in Apoptosis: Bcl-2 family Members and Mitochondrial Dynamics (2011, background): “Its insertion can be facilitated by the voltage-dependent anion channel isoform 2 with which it was found to interact (Cheng et al., 2003; Lazarou et al., 2010; Roy et al., 2009).”
• Multiple Functions of BCL-2 Family Proteins (2013, background): “BCL-2 proteins also bind to the mitochondrial metabolite channel VDAC (Cheng et al. 2003), autophagy regulator Beclin 1 (Pattingre et al.”
• Mitochondrial membrane permeabilization in cell death. (2007, background): “For instance, VDAC2 reportedly sequesters Bak by a direct molecular interaction, thus preventing Bak activation and apoptosis (121), whereas VDAC1 may serve as a receptor for Bax (597).”