Abstract:
:The caspases are cysteine proteases that have been implicated in the execution of programmed cell death in organisms ranging from nematodes to humans. Many members of the Bcl-2 family, including Bcl-XL, are potent inhibitors of programmed cell death and inhibit activation of caspases in cells. Here, we report a direct interaction between caspases and Bcl-XL. The loop domain of Bcl-XL is cleaved by caspases in vitro and in cells induced to undergo apoptotic death after Sindbis virus infection or interleukin 3 withdrawal. Mutation of the caspase cleavage site in Bcl-XL in conjunction with a mutation in the BH1 homology domain impairs the death-inhibitory activity of Bcl-XL, suggesting that interaction of Bcl-XL with caspases may be an important mechanism of inhibiting cell death. However, once Bcl-XL is cleaved, the C-terminal fragment of Bcl-XL potently induces apoptosis. Taken together, these findings indicate that the recognition/cleavage site of Bcl-XL may facilitate protection against cell death by acting at the level of caspase activation and that cleavage of Bcl-XL during the execution phase of cell death converts Bcl-XL from a protective to a lethal protein.
journal_name
Proc Natl Acad Sci U S Aauthors
Clem RJ,Cheng EH,Karp CL,Kirsch DG,Ueno K,Takahashi A,Kastan MB,Griffin DE,Earnshaw WC,Veliuona MA,Hardwick JMdoi
10.1073/pnas.95.2.554subject
Has Abstractpub_date
1998-01-20 00:00:00pages
554-9issue
2eissn
0027-8424issn
1091-6490journal_volume
95pub_type
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