Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
BCL-2, BCL-X-L sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis
Autore:
Cheng, EHYA; Wei, MC; Weiler, S; Flavell, RA; Mak, TW; Lindsten, T; Korsmeyer, SJ;
Indirizzi:
Harvard Univ, Sch Med, Dana Farber Canc Inst, Howard Hughes Med Inst, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 rd Hughes Med Inst, Boston, MA 02115 USA Yale Univ, Sch Med, Howard Hughes Med Inst, Immunobiol Sect, New Haven, CT06520 USA Yale Univ New Haven CT USA 06520 Immunobiol Sect, New Haven, CT06520 USA Ontario Canc Inst, Div Cellular & Mol Biol, Amgen Inst, Toronto, ON M5G 2M9, Canada Ontario Canc Inst Toronto ON Canada M5G 2M9 , Toronto, ON M5G 2M9, Canada Univ Penn, Dept Pathol & Lab Med, Abramson Family Canc Res Inst, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 Res Inst, Philadelphia, PA 19104 USA
Titolo Testata:
MOLECULAR CELL
fascicolo: 3, volume: 8, anno: 2001,
pagine: 705 - 711
SICI:
1097-2765(200109)8:3<705:BBSBDM>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROGRAMMED CELL-DEATH; CYTOCHROME-C; PROTEIN; FAMILY; ACTIVATION; BCL-X(L); MEMBRANE; ELEGANS; RELEASE; DIMERIZATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Korsmeyer, SJ Harvard Univ, Sch Med, Dana Farber Canc Inst, Howard Hughes Med Inst, 44 Binney St, Boston, MA 02115 USA Harvard Univ 44 Binney St Boston MA USA 02115 , MA 02115 USA
Citazione:
E.H.Y.A. Cheng et al., "BCL-2, BCL-X-L sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis", MOL CELL, 8(3), 2001, pp. 705-711

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-X-L 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 18:14:55