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Journal ArticleDOI

Beclin 1: a BH3-only protein that fails to induce apoptosis

TLDR
The intriguing finding that Bcl-2, as it interacts with Beclin 1, does not lose its anti-apoptotic potential may have far-reaching implications for the comprehension of the cross-talk between apoptosis and autophagy.
Abstract
Beclin 1 has been recently shown to possess a Bcl-2 homology-3 (BH3) domain that mediates its interaction with antiapoptotic multidomain proteins Unlike other BH3-only proteins, Beclin 1 fails to stimulate apoptosis when it is overexpressed In this issue of Oncogene, Ciechomska et al report the intriguing finding that Bcl-2, as it interacts with Beclin 1, does not lose its anti-apoptotic potential This finding may have far-reaching implications for the comprehension of the cross-talk between apoptosis and autophagy

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Bcl-2 and Bcl-xL play important roles in the crosstalk between autophagy and apoptosis

TL;DR: Bcl‐2 and Bcl‐xL, the well‐characterized apoptosis guards, appear to be important factors in autophagy, inhibiting Beclin 1‐mediated autophagic activity by binding to Becl in addition to cooperating with Atg5 or Ca2+ to regulate bothAutophagy and apoptosis.
Journal ArticleDOI

Cross talk between apoptosis and autophagy by caspase-mediated cleavage of Beclin 1

TL;DR: The significant finding that caspases can cleave Beclin 1, thereby destroying its pro-autophagic activity is reported, which provides important insights into the molecular cross talk between autophagy and apoptosis.
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The Autophagy Protein Atg12 Associates with Antiapoptotic Bcl-2 Family Members to Promote Mitochondrial Apoptosis

TL;DR: The essential autophagy protein Atg 12 is identified as a positive mediator of mitochondrial apoptosis and it is shown that Atg12 directly regulates the apoptotic pathway by binding and inactivating prosurvival B cl-2 family members, including Bcl-2 and Mcl-1.
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Stress-induced self-cannibalism: on the regulation of autophagy by endoplasmic reticulum stress

TL;DR: Current knowledge regarding how ER stress and the unfolded protein response (UPR) induce autophagy is reviewed, including description of the different autophagic-related genes which are regulated by the UPR.
References
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Journal ArticleDOI

Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy.

TL;DR: Bcl-2 not only functions as an antiapoptotic protein, but also as an antiautophagy protein via its inhibitory interaction with Beclin 1, which may help maintain autophagy at levels that are compatible with cell survival, rather than cell death.
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Induction of autophagy and inhibition of tumorigenesis by beclin 1.

TL;DR: It is shown that beclin 1 is a mammalian autophagy gene that can inhibit tumorigenesis and is expressed at decreased levels in human breast carcinoma, suggesting that decreased expression of Autophagy proteins may contribute to the development or progression of breast and other human malignancies.
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The Bcl-2 apoptotic switch in cancer development and therapy

TL;DR: Better understanding of the Bcl-2 family is clarifying its role in cancer development, revealing how conventional therapy works and stimulating the search for ‘BH3 mimetics’ as a novel class of anticancer drugs.
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Autophagic cell death: the story of a misnomer

TL;DR: This work evaluates the accumulating body of literature that argues that cell death occurs by autophagy and lists the caveats that must be considered when deciding whether or notAutophagy is an important effector mechanism of cell death.
Journal ArticleDOI

JNK1-Mediated Phosphorylation of Bcl-2 Regulates Starvation-Induced Autophagy

TL;DR: It is demonstrated that JNK1-mediated multisite phosphorylation of Bcl-2 stimulates starvation-induced autophagy by disrupting the B cl-2/Beclin 1 complex, which defines a mechanism that cells use to regulate autophagic activity in response to nutrient status.
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