An insight into the mechanistic role of Beclin 1 and its inhibition by prosurvival Bcl-2 family proteins

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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 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.
Publisher
LANDES BIOSCIENCE
Issue Date
2008-05
Language
English
Article Type
Article
Keywords

AUTOPHAGY; DOMAIN; COMPLEX; APOPTOSIS; BINDING; DEATH; UVRAG

Citation

AUTOPHAGY, v.4, no.4, pp.519 - 520

ISSN
1554-8627
URI
http://hdl.handle.net/10203/92872
Appears in Collection
BS-Journal Papers(저널논문)
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