BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly.

By T. Kuwana, L. Bouchier-Hayes, J. Chipuk, Christine Bonzon, B. Sullivan, Douglas R. Green, D. Newmeyer. Molecules and Cells, 2005

1,255 citations recorded by the source corpus.

Subfields: Molecular Biology, Nutrition and Dietetics

View Paper: https://www.semanticscholar.org/paper/0dea1db8f967df944194406a8bf529f073fe5f39

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. A. Letai
5. Suzanne Cory
6. R. Youle
7. A. Strasser
8. J. Chipuk

In Nutrition and Dietetics

1. Douglas R. Green
2. Guido Kroemer
3. A. Strasser

Citations in the corpus

• BCL-2 family antagonists for cancer therapy (2008, background): “Alternatively, some data support a direct interaction between certain BH3-only proteins and BA”
• Apoptosis: controlled demolition at the cellular level (2008, background): “BAX (BCL-2-associated X protein) and/or BAK (BCL-2-antagonist/killer-1) become activated early in apoptosis through the actions of one or more BH3-only proteins , and this results in permeabilization of mitochondrial outer membranes and release of mitochondrial intermembrane space protein”
• Glycogen synthase kinase-3 regulates mitochondrial outer membrane permeabilization and apoptosis by destabilization of MCL-1. (2006, background): “This is counteracted by antiapoptotic BCL-2 family members, mainly BCL-2, BCL-xL, and MCL-1, which sequester BAX- or BAKactivating BH3-only proteins BIM and BID (Cheng et al., 2001; Kuwana et al., 2005; Letai et al., 2002).”
• Neuronal Cell Death. (2018, neutral): “It is clear that different BH3-only proteins display selective binding to anti-apoptotic Bcl-2 family members (104, 344, 373).”
• The BH3 mimetic ABT-737 targets selective Bcl-2 proteins and efficiently induces apoptosis via Bak/Bax if Mcl-1 is neutralized. (2006, background): “ABT-737 does not activate Bax directly We next considered whether the drug could kill by directly activating Bax/Bak, as proposed for certain BH3-only proteins (Kuwana et al., 2005; Letai et al., 2002).”
• Anoikis molecular pathways and its role in cancer progression. (2013, background): “The sensitizer BH3-only proteins are unable to directly activate Bax and Bak oligomerization and contribute to cell death through the inactivation of the anti-apoptotic functions of Bcl-2, by competing for its BH3 binding domain, thus freeing activator BH3-only proteins to induce Bax– Bak oligomer f”
• Cell Death Signaling. (2015, background): “3C), although other conditions (such as heat, changes in pH, and changes in the lipid milieu) may activate the effectors independently of BH3-only proteins (Wei et al. 2000; Kuwana et al. 2002, 2005; Letai et al. 2002).”
• The BCL-2 Family Reunion (2010, background): “Similar evidence exists for BIMmediated BAK/BAX activation; and while PUMA was also suggested to promote BAK/BAX activation, this effect may not be direct (Chipuk et al., 2008; Kim et al., 2006; Kuwana et al., 2005; Letai et al., 2002).”
• Control of mitochondrial apoptosis by the Bcl-2 family (2009, background): “Apoptosis that is caused by BH3-only proteins absolutely requires Bax and Bak (Kuwana et al., 2005; Lindsten et al., 2000; Wei et al., 2000; Wei et al., 2001).”
• How does p53 induce apoptosis and how does this relate to p53-mediated tumour suppression? (2017, background): “Of note, NOXA preferentially inhibits MCL-1 and (in contrast to other BH3-only proteins that can bind to MCL-1) promotes the degradation of this pro-survival protein.(65,66) The prominent role of NOXA in UV radiation-induced apoptosis Mechanisms by which p53 induces cell death BJ Aubrey et al”
• Chronic lymphocytic leukemia requires BCL2 to sequester prodeath BIM, explaining sensitivity to BCL2 antagonist ABT-737. (2007, background): “Certain BH3 domains, such as BID and BIM, induce allosteric changes and oligomerization of BAX and BAK and are termed activators (8, 9).”
• Mitochondria in Apoptosis: Bcl-2 family Members and Mitochondrial Dynamics (2011, background): “Many groups have confirmed and extended these observations to other BH3-only proteins, including Bim and Puma (Gallenne et al., 2009; Kim et al., 2009; Kuwana et al., 2005; Mé rino et al., 2009; Ren et al., 2010).”
• Caspase-independent cell death (2005, background): “Recent studies indicate that BH3-only proteins fall into two subfamilies: those that can directly trigger opening of the Bax-Bak channel to precipitate MOMP, and those that sensitize for opening of the latter channel by neutralizing members of the Bcl-2 family that can inhibit channel openin”
• The role of mitochondria in apoptosis. (2008, background): “The pro-apoptotic members can be divided into two groups (22, 23): those with BH1, BH2 and BH3 domains, such as Bax and Bak, and”
• Mitochondrial outer membrane permeabilization during apoptosis: the innocent bystander scenario (2006, background): “proteins such as BCL-xL or MCL-1 and allowing for the subsequent release of previously inhibited direct activators (Figure 3c).(7,11) Evidence suggests that the BH3-only proteins,”