Functional and physical interaction between Bcl‐XL and a BH3‐like domain in Beclin‐1

By M. Maiuri, Gaëtane Le Toumelin, A. Criollo, J. Rain, F. Gautier, P. Juin, E. Tasdemir, G. Pierron, Kostoula Troulinaki, Nektarios Tavernarakis and 3 more. EMBO Journal, 2007

1,166 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/4c3bcdde3ac7e1f7bf6073d107df46a2f0932d09

How researchers see this paper

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In Cell Biology

1. Beth Levine
2. Guido Kroemer
3. Douglas R. Green
4. Alec C. Kimmelman
5. N. Mizushima
6. L. Galluzzi
7. D. Rubinsztein
8. P. Codogno

In Epidemiology

1. Guido Kroemer
2. Beth Levine
3. Douglas R. Green
4. N. Mizushima
5. L. Galluzzi
6. Alec C. Kimmelman
7. I. Slaninová
8. Guillermo Mariño

In Molecular Biology

1. Guido Kroemer
2. Beth Levine
3. Douglas R. Green
4. L. Galluzzi
5. Guillermo Mariño
6. N. Mizushima
7. Simone Fulda
8. Peter Vandenabeele

Citations in the corpus

• Autophagy and the integrated stress response (2010, positive): “Antiapoptotic family members (such as Bcl-2, Bcl-XL, and Mcl-1) are also important negative regulators of autophagy through an inhibitory interaction of their BH3-binding groove with the BH3 domain of Beclin 1 (Maiuri et al., 2007; Pattingre et al., 2005) (Figure 2B).”
• Cellular Stress Responses: Cell Survival and Cell Death (2010, background): “[56] M.”
• BCL-2 family antagonists for cancer therapy (2008, background): “Release of this interaction by competition with a BH3-only protein (or a small-molecule mimetic) has been found to stimulate autophag”
• JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy. (2008, background): “This latter model is attractive in view of recent structural evidence that the Bcl-2 binding site of Beclin 1 is a BH3 domain (Maiuri et al., 2007; Oberstein et al., 2007), since phosphorylation of Bcl-2 blocks its binding to other BH3-only containing proteins (Bassik et al., 2004).”
• DAP‐kinase‐mediated phosphorylation on the BH3 domain of beclin 1 promotes dissociation of beclin 1 from Bcl‐XL and induction of autophagy (2009, background): “…protein, and that the a-helix of its BH3 domain binds to the hydrophobic groove in Bcl-XL domain similarly to the interactions shown previously for the other BH3-domain-only proteins (Pattingre et al, 2005; Erlich et al, 2007; Feng et al, 2007; Oberstein et al, 2007; Maiuri et al, 2007a).”
• Cell Death Signaling. (2015, background): “Under stress conditions (e.g., starvation or hypoxia), the BH3-only proteins Bad and Bnip3 release beclin 1 to permit its participation in the autophagic process (Maiuri et al. 2007a,b; Bellot et al. 2009).”
• Hypoxia-Induced Autophagy Is Mediated through Hypoxia-Inducible Factor Induction of BNIP3 and BNIP3L via Their BH3 Domains (2009, background): “Although we have not been able to measure the affinity of these BNIP BH3 peptides for Bcl-XL, we propose that their affinity is low, like that of the BH3 domain of Beclin1 ( 18 , 23).”