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Aven, a Novel Inhibitor of Caspase Activation, Binds Bcl-xL and Apaf-1

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CHAU, B·2000·Molecular Cell
DOI 10.1016/s1097-2765(00)00005-8
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Abstract

Bcl-x(L), an antiapoptotic Bcl-2 family member, is postulated to function at multiple stages in the cell death pathway. The possibility that Bcl-x(L) inhibits cell death at a late (postmitochondrial) step in the death pathway is supported by this report of a novel apoptosis inhibitor, Aven, which binds to both Bcl-x(L) and the caspase regulator, Apaf-1. Identified in a yeast two-hybrid screen, Aven is broadly expressed and is conserved in other mammalian species. Only those mutants of Bcl-x(L)that retain their antiapoptotic activity are capable of binding Aven. Aven interferes with the ability of Apaf-1 to self-associate, suggesting that Aven impairs Apaf-1-mediated activation of caspases. Consistent with this idea, Aven inhibited the proteolytic activation of caspases in a cell-free extract and suppressed apoptosis induced by Apaf-1 plus caspase-9. Thus, Aven represents a new class of cell death regulator.

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Metadata

Authors
CHAU, B.
Venue
Molecular Cell
Publisher
Elsevier BV
Published
2000-07
Volume
6
Issue
1
Pages
31-40
ISSN
1097-2765 (ISSN-L)
DOI
10.1016/s1097-2765(00)00005-8
OpenAlex
W2142146322
Cited by
213
References
2
FWCI
4.06
Type
journal article
Language
en
Open access
bronze
Licence

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CoChat. (2026). Citation check: Aven, a Novel Inhibitor of Caspase Activation, Binds Bcl-xL and Apaf-1. https://app.cochat.ai/papers/10.1016/s1097-2765(00)00005-8
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CHAU, B. (2000). Aven, a Novel Inhibitor of Caspase Activation, Binds Bcl-xL and Apaf-1. Molecular Cell. https://doi.org/10.1016/s1097-2765(00)00005-8

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