Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis
Autore:
Bae, J; Hsu, SY; Leo, CP; Zell, K; Hsueh, AJW;
Indirizzi:
Stanford Univ, Sch Med, Dept Gynecol & Obstet, Div Reprod Biol, Stanford, CA 94305 USA Stanford Univ Stanford CA USA 94305 v Reprod Biol, Stanford, CA 94305 USA
Titolo Testata:
APOPTOSIS
fascicolo: 5, volume: 6, anno: 2001,
pagine: 319 - 330
SICI:
1360-8185(200110)6:5<319:UBIWDA>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
SURVIVAL-PROMOTING PROTEINS; PROGRAMMED CELL-DEATH; BH3 DOMAIN; X-L; MAMMALIAN-CELLS; CYTOCHROME-C; AGONIST BAD; RAT OVARY; IN-VIVO; PHOSPHORYLATION;
Keywords:
apoptosis; Bcl-2; BAD; phosphorylation; programmed cell death; yeast two-hybrid;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
53
Recensione:
Indirizzi per estratti:
Indirizzo: Hsueh, AJW Stanford Univ, Sch Med, Dept Gynecol & Obstet, Div Reprod Biol,300 Pasteur Dr,Room A344, Stanford, CA 94305 USA Stanford Univ 300 PasteurDr,Room A344 Stanford CA USA 94305 SA
Citazione:
J. Bae et al., "Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis", APOPTOSIS, 6(5), 2001, pp. 319-330

Abstract

Survival factors activate kinases which, in turn, phosphorylate the proapoptotic Bcl-xl/Bcl-2-associated death promoter homolog (BAD) protein at key serine residues. Phosphorylated BAD interacts with 14-3-3 proteins, and overexpression of 14-3-3 attenuates BAD-mediated apoptosis. Although BAD is known to interact with Bcl-2, Bcl-w, and Bcl-xL, the exact relationship between BAD and anti- or proapoptotic Bcl-2 proteins has not been analyzed systematically. Using the yeast two-hybrid protein interaction assay, we found that BAD interacted negligibly with proapoptotic Bcl-2 proteins. Even thoughwild type BAD only interacted with selected numbers of antiapoptotic proteins, underphosphorylated mutant BAD interacted with all antiapoptotic Bcl-2proteins tested (Bcl-2, Bcl-w, Bcl-xL, Bfl-1/A1, Mcl-1, Ced-9, and BHRF-1). Using nonphosphorylated recombinant BAD expressed in bacteria, direct interactions between BAD and diverse antiapoptotic Bcl-2 members were also observed. Furthermore, apoptosis induced by BAD was blocked by coexpression with Bcl-2, Bcl-w, and Bfl-1. Comparison of BAD orthologs from zebrafish to human indicated the conservation of a 14-3-3 binding site and the BH3 domainduring evolution. Thus, highly conserved BAD interacts with diverse antiapoptotic Bcl-2 members to regulate apoptosis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 00:37:10