Abstract：
:Apoptosis and autophagy are both tightly regulated biological processes that play a central role in tissue homeostasis, development, and disease. The anti-apoptotic protein, Bcl-2, interacts with the evolutionarily conserved autophagy protein, Beclin 1. However, little is known about the functional significance of this interaction. Here, we show that wild-type Bcl-2 antiapoptotic proteins, but not Beclin 1 binding defective mutants of Bcl-2, inhibit Beclin 1-dependent autophagy in yeast and mammalian cells and that cardiac Bcl-2 transgenic expression inhibits autophagy in mouse heart muscle. Furthermore, Beclin 1 mutants that cannot bind to Bcl-2 induce more autophagy than wild-type Beclin 1 and, unlike wild-type Beclin 1, promote cell death. Thus, Bcl-2 not only functions as an antiapoptotic protein, but also as an antiautophagy protein via its inhibitory interaction with Beclin 1. This antiautophagy function of Bcl-2 may help maintain autophagy at levels that are compatible with cell survival, rather than cell death.
journal_name
Celljournal_title
Cellauthors
Pattingre S,Tassa A,Qu X,Garuti R,Liang XH,Mizushima N,Packer M,Schneider MD,Levine Bdoi
10.1016/j.cell.2005.07.002subject
Has Abstractpub_date
2005-09-23 00:00:00pages
927-39issue
6eissn
0092-8674issn
1097-4172pii
S0092-8674(05)00692-6journal_volume
122pub_type
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