An insight into the mechanistic role of Beclin 1 and its inhibition by prosurvival Bcl-2 family proteins
SCIE
SCOPUS
- Title
- An insight into the mechanistic role of Beclin 1 and its inhibition by prosurvival Bcl-2 family proteins
- Authors
- Ku, B; Woo, JS; Liang, C; Lee, KH; Jung, JU; Oh, BH
- Date Issued
- 2008-05-16
- Publisher
- LANDES BIOSCIENCE
- Abstract
- 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 gamma-herpesvirus 68, known as M 11, binds to Beclin 1 with markedly high affinity in comparison with cellular Bcl-2 or Bcl-X-L 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 I forms a large homo-oligomer, and this oligornerization 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.
- Keywords
- autophagy; Beclin 1; Bcl-2; M 11; oligoincrization; AUTOPHAGY; DOMAIN; COMPLEX; APOPTOSIS; BINDING; DEATH; UVRAG
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/22756
- DOI
- 10.4161/auto.5846
- ISSN
- 1554-8627
- Article Type
- Article
- Citation
- AUTOPHAGY, vol. 4, no. 4, page. 519 - 520, 2008-05-16
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- There are no files associated with this item.
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