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- Publisher Website: 10.1016/S1097-2765(01)00320-3
- Scopus: eid_2-s2.0-0034786019
- PMID: 11583631
- WOS: WOS:000171251500024
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Article: BCL-2, BCL-XL sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis
Title | BCL-2, BCL-X<inf>L</inf> sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis |
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Authors | |
Issue Date | 2001 |
Citation | Molecular Cell, 2001, v. 8, n. 3, p. 705-711 How to Cite? |
Abstract | Critical issues in apoptosis include the importance of caspases versus organelle dysfunction, dominance of anti- versus proapoptotic BCL-2 members, and whether commitment occurs upstream or downstream of mitochondria. Here, we show cells deficient for the downstream effectors Apaf-1, Caspase-9, or Caspase-3 display only transient protection from "BH3 domain-only" molecules and die a caspase-independent death by mitochondrial dysfunction. Cells with an upstream defect, lacking "multidomain" BAX, BAK demonstrate long-term resistance to all BH3 domain-only members, including BAD, BIM, and NOXA. Comparison of wild-type versus mutant BCL-2, BCL-XL indicates these antiapoptotics sequester BH3 domain-only molecules in stable mitochondrial complexes, preventing the activation of BAX, BAK. Thus, in mammals, BH3 domain-only molecules activate multidomain proapoptotic members to trigger a mitochondrial pathway, which both releases cytochrome c to activate caspases and initiates caspase-independent mitochondrial dysfunction. |
Persistent Identifier | http://hdl.handle.net/10722/291553 |
ISSN | 2023 Impact Factor: 14.5 2023 SCImago Journal Rankings: 9.332 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Cheng, Emily H.Y. | - |
dc.contributor.author | Wei, Michael C. | - |
dc.contributor.author | Weiler, Solly | - |
dc.contributor.author | Flavell, Richard A. | - |
dc.contributor.author | Mak, Tak W. | - |
dc.contributor.author | Lindsten, Tullia | - |
dc.contributor.author | Korsmeyer, Stanley J. | - |
dc.date.accessioned | 2020-11-17T14:54:37Z | - |
dc.date.available | 2020-11-17T14:54:37Z | - |
dc.date.issued | 2001 | - |
dc.identifier.citation | Molecular Cell, 2001, v. 8, n. 3, p. 705-711 | - |
dc.identifier.issn | 1097-2765 | - |
dc.identifier.uri | http://hdl.handle.net/10722/291553 | - |
dc.description.abstract | Critical issues in apoptosis include the importance of caspases versus organelle dysfunction, dominance of anti- versus proapoptotic BCL-2 members, and whether commitment occurs upstream or downstream of mitochondria. Here, we show cells deficient for the downstream effectors Apaf-1, Caspase-9, or Caspase-3 display only transient protection from "BH3 domain-only" molecules and die a caspase-independent death by mitochondrial dysfunction. Cells with an upstream defect, lacking "multidomain" BAX, BAK demonstrate long-term resistance to all BH3 domain-only members, including BAD, BIM, and NOXA. Comparison of wild-type versus mutant BCL-2, BCL-XL indicates these antiapoptotics sequester BH3 domain-only molecules in stable mitochondrial complexes, preventing the activation of BAX, BAK. Thus, in mammals, BH3 domain-only molecules activate multidomain proapoptotic members to trigger a mitochondrial pathway, which both releases cytochrome c to activate caspases and initiates caspase-independent mitochondrial dysfunction. | - |
dc.language | eng | - |
dc.relation.ispartof | Molecular Cell | - |
dc.title | BCL-2, BCL-X<inf>L</inf> sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis | - |
dc.type | Article | - |
dc.description.nature | link_to_OA_fulltext | - |
dc.identifier.doi | 10.1016/S1097-2765(01)00320-3 | - |
dc.identifier.pmid | 11583631 | - |
dc.identifier.scopus | eid_2-s2.0-0034786019 | - |
dc.identifier.volume | 8 | - |
dc.identifier.issue | 3 | - |
dc.identifier.spage | 705 | - |
dc.identifier.epage | 711 | - |
dc.identifier.isi | WOS:000171251500024 | - |
dc.identifier.issnl | 1097-2765 | - |