The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.
Bcl-2 family members: Dual regulators of apoptosis and autophagy
Open accessAbstract
The essential autophagy protein and haplo-insufficient tumor suppressor, Beclin 1, interacts with several cofactors (Ambra1, Bif-1, UVRAG) to activate the lipid kinase Vps34, thereby inducing autophagy. In normal conditions, Beclin 1 is bound to and inhibited by Bcl-2 or the Bcl-2 homolog Bcl-X(L). This interaction involves a Bcl-2 homology 3 (BH3) domain in Beclin 1 and the BH3 binding groove of Bcl-2/Bcl-X(L). Other proteins containing BH3 domains, called BH3-only proteins, can competitively disrupt the interaction between Beclin 1 and Bcl-2/Bcl-X(L) to induce autophagy. Nutrient starvation, which is a potent physiologic inducer of autophagy, can stimulate the dissociation of Beclin 1 from its inhibitors, either by activating BH3-only proteins (such as Bad) or by posttranslational modifications of Bcl-2 (such as phosphorylation) that may reduce its affinity for Beclin 1 and BH3-only proteins. Thus, anti-apoptotic Bcl-2 family members and pro-apoptotic BH3-only proteins may participate in the inhibition and induction of autophagy, respectively. This hitherto neglected crosstalk between the core machineries regulating autophagy and apoptosis may redefine the role of Bcl-2 family proteins in oncogenesis and tumor progression.
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Metadata
- Authors
- Levine, B., Sinha, S. C., & Kroemer, G.
- Venue
- Autophagy
- Publisher
- Informa UK Limited
- Published
- 2008-05-22
- Volume
- 4
- Issue
- 5
- Pages
- 600-606
- ISSN
- 1554-8627 (ISSN-L)
- 1554-8635
- OpenAlex
- W2095240020
- Cited by
- 834
- References
- 62
- FWCI
- 41.83
- Type
- journal article
- Language
- en
- Open access
- hybrid
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