Direct Activation of Bax by p53 Mediates Mitochondrial Membrane Permeabilization and Apoptosis

By J. Chipuk, T. Kuwana, L. Bouchier-Hayes, N. Droin, D. Newmeyer, M. Schuler, Douglas R. Green. Science, 2004

2,147 citations recorded by the source corpus.

Subfields: Biotechnology, Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/8ac054acf921abc9f97df5fd7ea018d60ed0c524

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Citations in the corpus

Apoptosis and Molecular Targeting Therapy in Cancer (2014, background): “As recently summarized, antiapoptotic proteins prevent Bax/Bak activation by sequestering/inhibiting “activator” BH3-only proteins and/or directly inhibiting Bax/Bak activation [33].”
The Tumor Suppressor Protein p53 and the Ferroptosis Network (2018, positive): “For example, cytosolic p53 can directly bind to pro-apoptotic members of the BCL-2 family (BAX [BCL2 associated X, apoptosis regulator] and BBC3/PUMA [BCL2 binding component 3]) to increase mitochondrial membrane permeabilization and the release of pro-apoptotic factors from the mitochondria [4,5].”
Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis. (2006, background): “In addition, p53 also transactivatesthemdm2genetoinitiatethep53-Mdm2feedback loop, which is crucial for restraining p53 function during the stress response (Michael and Oren, 2002; Brooks and Gu, 2006 ).”
Mitochondrial membrane permeabilization in cell death. (2007, background): “p53 might also activate the pore-forming, MMP-inducing function of Bax (131) or Bak (443).”
BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly. (2005, background): “For example, family proteins, although regulatory partners outside the family may also be important (Chipuk et al., 2004; Cud-E -Myc tumor cells can undergo apoptosis when Bcl-2 is downregulated (Letai et al., 2004). deback et al., 2001; Guo et al., 2003; Sawada et al., 2003).”
Bcl-2 family proteins and cancer (2008, background): “…with pro- and antiapoptotic Bcl-2-family proteins have been observed, directly modulating the bioactivities of the p21-Bax and p26-Bcl-2 proteins, and suggesting that p53 regulates the Bcl-2 family at both transcriptional and post-transcriptional levels (Chipuk et al., 2004; Deng et al., 2006).”
Control of mitochondrial apoptosis by the Bcl-2 family (2009, background): “In fact, there are data that support the role of Puma, p53 and heat as activators of Bax and Bak (Chipuk et al., 2004; Kim et al., 2006; Pagliari et al., 2005), and possibly others remain undiscovered.”
Mitochondria in Apoptosis: Bcl-2 family Members and Mitochondrial Dynamics (2011, background): “Other triggers, including BH3-only proteins, prostaglandins (Lalier et al., 2011), p53 (Chipuk et al., 2004), pH variations (Khaled et al., 1999), or posttranslational modifications (Kutuk and Letai, 2008), all could also be responsible for sending Bax to the OMM.”
Mitochondria in cancer cells: what is so special about them? (2008, positive): “Interestingly, p53 can also regulate OMM permeabilization through direct activation of Bax [ 68 ].”
Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy (2006, background): “…of the outer mitochondrial membrane in a transcriptionindependent fashion through direct activation of proapoptotic Bcl-2 proteins Bax or Bak or through binding and inactivating of antiapoptotic Bcl-2 proteins such as Bcl-2 or Bcl-XL (Mihara et al., 2003; Chipuk et al., 2004; Moll et al., 2005).”