Abstract:
:Human Bfl-1 is an anti-apoptotic Bcl-2 family member. Here, we found that Bfl-1 was converted into a potent death-promoting protein by green fluorescent protein (GFP) fusion with its N-terminus. The transient expression of GFP-Bfl-1 induced cytochrome c release and triggered apoptosis in 293T cells, which depended on the mitochondrial localization of GFP-Bfl-1. Apoptosis induced by GFP-Bfl-1 was significantly blocked by the pan-caspase inhibitor carbobenzoxy-Val-Ala-Asp-fluoromethyl ketone, but was not blocked by either Bcl-xL or Bfl-1. Our findings provide a useful model for understanding the structural basis of Bcl-2 family proteins that act in an opposite way despite sharing structural similarity between anti-apoptotic and pro-apoptotic proteins.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Ko JK,Choi KH,Kim HJ,Choi HY,Yeo DJ,Park SO,Yang WS,Kim YN,Kim CWdoi
10.1016/s0014-5793(03)00872-xkeywords:
subject
Has Abstractpub_date
2003-09-11 00:00:00pages
29-36issue
1-3eissn
0014-5793issn
1873-3468pii
S001457930300872Xjournal_volume
551pub_type
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