The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Differential Interactions Between Beclin 1 and Bcl-2 Family Members
Open accessAbstract
Autophagy, a cellular degradation system, promotes both cell death and survival. The interaction between Bcl-2 family proteins and Beclin 1, a Bcl-2 interacting protein that promotes autophagy, can mediate crosstalk between autophagy and apoptosis. We investigated the interaction between anti-and pro-apoptotic Bcl-2 proteins with Beclin 1. Our results show that Beclin 1 directly interacts with Bcl-2, Bcl-x(L), Bcl-w and to a lesser extent with Mcl-1. Beclin 1 does not bind the pro-apoptotic Bcl-2 proteins. The interaction between Beclin 1 and the anti-apoptotic protein Bcl-x(L) was inhibited by BH3-only proteins, but not by multi-domain proteins. Sequence alignment and structural modeling suggest that Beclin 1 contains a putative BH3-like domain which may interact with the hydrophobic grove of Bcl-x(L). Mutation of the Beclin 1 amino acids predicted to mediate this interaction inhibited the association of Beclin 1 with Bcl-x(L). Our results suggest that BH3 only proapoptotic Bcl-2 proteins may modulate the interactions between Bcl-x(L) and Beclin 1.
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Metadata
- Authors
- Erlich, S., Mizrachy, L., Segev, O., Lindenboim, L., Zmira, O., Adi-Harel, S., Hirsch, J. A., Stein, R., & Pinkas-Kramarski, R.
- Venue
- Autophagy
- Publisher
- Informa UK Limited
- Published
- 2007-11-26
- Volume
- 3
- Issue
- 6
- Pages
- 561-568
- ISSN
- 1554-8627 (ISSN-L)
- 1554-8635
- OpenAlex
- W1964032090
- Cited by
- 292
- References
- 6
- FWCI
- 5.75
- Type
- journal article
- Language
- en
- Open access
- bronze
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