BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak

Genes and Development

Volumn 15, Issue 12, 2001, Pages 1481-1486

  Zong, Wei Xing ^a   Lindsten, Tullia ^a   Ross, Andrea J ^b   MacGregor, Grant R ^b   Thompson, Craig B ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Bad; Bak; Bax; Bcl 2; BH3 only; Bim

Indexed keywords

ANTINEOPLASTIC AGENT; BIM PROTEIN; CELL PROTEIN; PROTEIN BAD; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; PROTEIN P53; UNCLASSIFIED DRUG;

ANIMAL CELL; APOPTOSIS; ARTICLE; CARCINOGENESIS; CELL LINE; CONTROLLED STUDY; FIBROBLAST; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; SENSITIZATION; ULTRAVIOLET IRRADIATION;

ANIMALS; APOPTOSIS; APOPTOSIS REGULATORY PROTEINS; BCL-2 HOMOLOGOUS ANTAGONIST-KILLER PROTEIN; BCL-2-ASSOCIATED X PROTEIN; BCL-ASSOCIATED DEATH PROTEIN; CARRIER PROTEINS; CELL TRANSFORMATION, NEOPLASTIC; CELLS, CULTURED; MEMBRANE PROTEINS; MICE; MUTAGENESIS; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-BCL-2;

ANIMALIA;

EID: 0035876483     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.897601     Document Type: Article

References (34)

1. The Bcl-2 protein family: Arbiters of cell survival
2. The protein Bcl-2 alpha does not require membrane attachment, but two conserved domains to suppress apoptosis
3. Akt phosphorylation of BAD couples survival signals to the cell- intrinsic death machinery
4. A matter of life and cell death
5. Structure-function analysis of Bcl-2 protein. Identification of conserved domains important for homodimerization with Bcl-2 and heterodimerization with Bax
6. Bok is a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective antiapoptotic Bcl-2 family members
7. Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis
8. BH3-Only proteins-essential initiators of apoptotic cell death
9. Role of Bak in UV-induced apoptosis in skin cancer and abrogation by HPV E6 proteins
10. Bax- and Bak-induced cell death in the fission yeast Schizosaccharomyces pombe
11. Bax directly induces release of cytochrome c from isolated mitochondria
12. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
13. The combined functions of proapoptotic Bcl-2 family members bak and bax are essential for normal development of multiple tissues
14. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
15. bax-deficiency promotes drug resistance and oncogenic transformation by attenuating p53-dependent apoptosis
16. Tumor suppressor p53 is a direct transcriptional activator of the human bax gene
17. PUMA, a novel proapoptotic gene, is induced by p53
18. Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria
19. Conformation of the Bax C-terminus regulates subcellular location and cell death
20. Bim: A novel member of the Bcl-2 family that promotes apoptosis
21. Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis
22. TNF-a signals apoptosis through a Bid-dependent conformational change in Bax that is inhibited by E1B 19K
23. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
24. Somatic frameshift mutations in the BAX gene in colon cancers of the microsatellite mutator phenotype
25. Downregulation of the pro-apoptotic protein Bak is required for the ras- induced transformation of intestinal epithelial cells
26. Bcl-2 and Fas/APO-1 regulate distinct pathways to lymphocyte apoptosis
27. Phosphorylation of the pro-apoptotic protein BAD on serine 155, a novel site, contributes to cell survival
28. tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
29. Proapoptotic Bax and Bak: A requisite gateway to mitochondrial dysfunction and death
30. Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death
31. PUMA induces the rapid apoptosis of colorectal cancer cells
32. Heterodimerization-independent functions of cell death regulatory proteins Bax and Bcl-2 in yeast and mammalian cells
33. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
34. Role of BAX in the apoptotic response to anticancer agents