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, Byung Ha Oh

Research output: Contribution to journalArticle

33 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)519-520
Number of pages2
Issue number4
Publication statusPublished - 2008 May 16
Externally publishedYes



  • Autophagy
  • Bcl-2
  • Beclin 1
  • M11
  • Oligomerization

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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