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Research Paper
Differential Interactions Between Beclin 1 and Bcl-2 Family Members
Shlomit Erlich, Liat Mizrachy, Oshik Segev, Liora Lindenboim, Ofir Zmira, Sheli Adi-Harel, Joel A. Hirsch, Reuven Stein and Ronit Pinkas-Kramarski
volume 3 | issue 6
November/December 2007Pages: 561 - 568
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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-xL, 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-xL 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-xL. Mutation of the Beclin 1 amino acids predicted to mediate this interaction inhibited the association of Beclin 1 with Bcl-xL. Our results suggest that BH3 only proapoptotic Bcl-2 proteins may modulate the interactions between Bcl-xL and Beclin 1.
Authors
Shlomit Erlich
Tel-Aviv University
Liat Mizrachy
Tel-Aviv University
Oshik Segev
Tel-Aviv University
Liora Lindenboim
Tel-Aviv University
Ofir Zmira
Tel-Aviv University
Sheli Adi-Harel
Tel-Aviv University
Joel A. Hirsch
Tel-Aviv University
Reuven Stein
Tel-Aviv University
Ronit Pinkas-Kramarski
Tel Aviv University
We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:
Download PDF If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.