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Article Addendum
An insight into the mechanistic role of Beclin 1 and its inhibition by prosurvival Bcl-2 family proteins
Bonsu Ku, Jae-Sung Woo, Chengyu Liang, Kwang-Hoon Lee, Jae U. Jung and Byung-Ha Oh
volume 4 | issue 4
16 May 2008Pages: 519 - 520
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A multiprotein complex composed of Beclin 1, PI(3)KC3 and UVRAG promotes autophagosome formation, while this activity is suppressed by a cohort of antiapoptotic Bcl-2 family members. Recently, we showed that a viral Bcl-2 of murine γ-herpesvirus 68, known as M11, binds to Beclin 1 with markedly high affinity in comparison with cellular Bcl-2 or Bcl-XL that interacts with Beclin 1 weakly.1 Furthermore, the binding affinity directly correlated with the potency of inhibition of autophagosome formation in cells. Herein, we present additional data showing that Beclin 1 forms a large homo-oligomer, and this oligomerization is partly disrupted by the binding of M11. Oligomerized Beclin 1 is proposed to serve as a platform enabling a concerted action of many molecules of the associating proteins, including Bif-1 that could be directly involved in autophagosome biogenesis on membranes owing to its BAR domain.
Addendum to: Ku B, Woo J-S, Liang C, Lee K-H, Hong H-S, Xiaofei E, Kim K-S, Jung JU, Oh B-H. Structural and biochemical bases for the inhibition of autophagy and apoptosis by viral BCL-2 of murine γ-herpesvirus 68. PLoS Pathog 2008; 4:e25.
Authors
Bonsu Ku
Pohang University of Science and Technology
Jae-Sung Woo
Pohang University of Science and Technology
Chengyu Liang
Department of Molecular Microbiology and Immunology, University of Southern California, Los Angeles, California USA
Kwang-Hoon Lee
Pohang University of Science and Technology
Jae U. Jung
1Department of Molecular Microbiology and Immunology, University of Southern California, Los Angeles, California USA
Byung-Ha Oh
Pohang University of Science and Technology