Double identity for proteins of the Bcl-2 family (original) (raw)
References
Tsujimoto, Y. & Croce, C. M. Analysis of the structure, transcripts, and protein products of bcl-2, the gene involved in human follicular lymphoma. Proc. Natl Acad. Sci. USA83, 5214–5218 (1986). ArticleADSCAS Google Scholar
Muchmore, S. W. et al. X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death. Nature381, 335–341 (1996). ArticleADSCAS Google Scholar
Baffy, G., Miyashita, T., Williamson, J. R. & Reed, J. C. Apoptosis induced by withdrawal of interleukin-3 (IL-3) from an IL-3-dependent hematopoietic cell line is associated with repartitioning of intracellular calcium and is blocked by enforced Bcl-2 oncoprotein production. J. Biol. Chem.268, 6511–6519 (1993). CASPubMed Google Scholar
Lam, M. et al. Evidence that Bcl-2 represses apoptosis by regulating endoplasmic reticulum-associated Ca2+fluxes. Proc. Natl Acad. Sci. USA91, 6569–6573 (1994). ArticleADSCAS Google Scholar
Ryan, J. J. et al. c-myc and bcl-2 modulate p53 function by altering p53 subcellular trafficking during the cell cycle. Proc. Natl Acad. Sci. USA91, 5878–5882 (1994). ArticleADSCAS Google Scholar
Minn, A. J. et al. Bcl-xLforms an ion channel in synthetic lipid membranes. Nature385, 353–357 (1997). ArticleADSCAS Google Scholar
Schendel, S. L. et al. Channel formation by anti-apoptotic protein, Bcl-2. Proc. Natl Acad. Sci. USA94, 5113–5118 (1997). ArticleADSCAS Google Scholar
Montal, M. Protein folds in channel structure. Curr. Opin. Struct. Biol.6, 499–510 (1996). ArticleCAS Google Scholar
Chen, J. et al. bcl-2 overexpression reduces apoptotic photoreceptor cell death in three different retinal degenerations. Proc. Natl Acad. Sci. USA93, 7042–7047 (1996). ArticleADSCAS Google Scholar
Middleton, G., Nunez, G. & Davies, A. M. Bax promotes neuronal survival and antagonises the survival effects of neurotrophic factors. Development122, 695–701 (1996). CASPubMed Google Scholar
Kiefer, M. C. et al. Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak. Nature374, 736–739 (1995). ArticleADSCAS Google Scholar
Bernardi, P., Broekemeier, K. M. & Pfeiffer, D. R. Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane. J. Bioenerget. Biomembr.26, 509–517 (1994). ArticleCAS Google Scholar
Zoratti, M. & Szabo, I. Electrophysiology of the inner mitochondrial membrane. J. Bioenerget. Biomembr.26, 543–553 (1996). Article Google Scholar
Petit, P. X., Susin, S.-A., Zamzami, N., Mignotte, B. & Kroemer, G. Mitochondria and programmed cell death: back ot the future. FEBS Lett.396, 7–13 (1996). ArticleCAS Google Scholar
Susin, S. A. et al. Bcl-2 inhibits the mitochondrial release of an apoptogenic protease. J. Exp. Med.184, 1331–1342 (1996). ArticleCAS Google Scholar
Xiang, J., Chao, D. T. & Korsmeyer, S. J. BAX-induced cell death may not require interleukin 1β-converting enzyme-like proteases. Proc. Natl Acad. Sci. USA93, 14559–14563 (1996). ArticleADSCAS Google Scholar
Kluck, R. M., Bossy-Wetzel, E., Green, D. R. & Newmeyer, D. D. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science275, 1132–1136 (1997). ArticleCAS Google Scholar
Yang, J. et al. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science275, 1129–1132 (1997). ArticleCAS Google Scholar
Häcker, G. & Vaux, D. L. Asticky business. Curr. Biol.5, 622–624 (1995). Article Google Scholar
Yuan, J. Y. & Horvitz, H. R. The Caenorhabditis elegans genes ced-3 and ced-4 act cell autonomously to cause programmed cell death. Dev. Biol.138, 33–41 (1990). ArticleCAS Google Scholar
Shaham, S. & Horvitz, H. R. Developing Caenorhabditis elegans neurons may contain both cell-death protective and killer activities. Genes Dev.10, 578–591 (1996). ArticleCAS Google Scholar
Spector, M. S., Desnoyers, S., Heoppner, D. J. & Hengartner, M. O. Interaction between the C. elegans cell-death regulators CED-9 and CED-4. Nature275, 1122–1126 (1997). Google Scholar
Chinnaiyan, A. M., O'Rourke, K., Lane, B. R. & Dixit, V. M. Interaction of CED-4 with CED-3 and CED-9: a molecular framework for cell death. Science275, 1122–1126 (1997). ArticleCAS Google Scholar
Wu, D., Wallen, H. D. & Nunez, G. Interaction and regulation of subcellular localization of CED-4 by CED-9. Science275, 1126–1129 (1997). ArticleCAS Google Scholar
Shaham, S. & Horvitz, H. R. An alternatively spliced C. elegans ced-4 RNA encodes a novel cell death inhibitor. Cell86, 201–208 (1996). ArticleCAS Google Scholar
Wang, H. G., Rapp, U. R. & Reed, J. C. Bcl-2 targets the protein kinase Raf-1 to mitochondria. Cell87, 629–638 (1996). ArticleCAS Google Scholar
Zha, J., Harada, H., Yang, E., Jockel, J. & Korsmeyer, S. J. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3–3 not BCL-XL. Cell87, 619–628 (1996). ArticleCAS Google Scholar
Wang, H.-G., Takayama, S., Rapp, U. R. & Reed, J. C. Bcl-2 interacting protein, BAG-1, binds to and activates the kinase Raf-1. Proc. Natl Acad. Sci. USA93, 7063–7068 (1996). ArticleADSCAS Google Scholar
Sattler, M. et al. Structure of Bcl-xL–Bak peptide complex: recognition between regulators of apoptosis. Science275, 983–986 (1997). ArticleCAS Google Scholar
Diaz, J.-L. et al. Acommon binding site mediates heterodimerization and homodimerization of Bcl-2 family members. J. Biol. Chem.272, 11350–11355 (1997). ArticleCAS Google Scholar
Shibasaki, F., Kondo, E., Akagi, T. & McKeon, F. Suppression of signalling through NF-AT by interactions between calcineurin and Bcl-2. Nature386, 728–731 (1997). ArticleADSCAS Google Scholar
Shibasaki, F. & McKeon, F. Calcineurin functions in Ca2+-activated cell death in mammalian cells. J. Cell Biol.131, 735–743 (1995). ArticleCAS Google Scholar
Pietenpol, J. A. et al. Paradoxical inhibition of solid tumor cell growth by bcl-2. Cancer Res.54, 3714–3717 (1994). CASPubMed Google Scholar
Linette, G. P., Li, Y., Roth, K. & Korsmeyer, S. J. Cross talk between cel death and cell cycle progression: BCL-2 regulates NFAT-medicated activation. Proc. Natl Acad. Sci. USA93, 9545–9552 (1996). ArticleADSCAS Google Scholar
Huang, D. C. S., O'Reilly, L. A., Strasser, & Cory, S. The anti-apoptosis function of Bcl-2 can be genetically separated from its inhibitory effect on cell cycle entry. EMBO J.(in the press).
Haldar, S., Jena, N. & Croce, C. M. Inactivation of Bcl-2 by phosphorylation. Proc. Natl Acad. Sci. USA92, 4507–4511 (1995). ArticleADSCAS Google Scholar
Chang, B. S., Minn, A. J., Muchmore, S. W., Fesik, S. W. & Thompson, C. B. Identification of a novel regulatory domain in Bcl-xLand Bcl-2. EMBO J.16, 968–977 (1997). ArticleCAS Google Scholar
Naumovski, L. & Cleary, M. L. The p53-binding protein 53BP2 also interacts with Bcl-2 and impedes cell cycle progression at G2/M. Mol. Cell. Biol.16, 3884–3892 (1996). ArticleCAS Google Scholar
Krajewski, S. et al. Investigations of the subcellular distribution of the bcl-2 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes. Cancer Res.53, 4701–4714 (1993). CASPubMed Google Scholar
Kane, D. J., örd, T., Anton, R. & Bredesen, D. E. Expression of Bcl-2 inhibits necrotic neural cell death. J. Neurosci. Res.40, 269–275 (1995). ArticleCAS Google Scholar