Identification of Novel Isoforms of the BH3 Domain Protein Bim Which Directly Activate Bax To Trigger Apoptosis

REFERENCES

• Adams, J. M., and S. Cory. 2001. Life-or-death decisions by the Bcl-2 protein family. Trends Biochem. Sci. 26: 61–66.
   PubMed Web of Science ®Google Scholar
• Antonsson, B., and J. C. Martinou. 2000. The Bcl-2 protein family. Exp. Cell Res. 256: 50–57.
   PubMed Web of Science ®Google Scholar
• Bae, J., C. P. Leo, S. Y. Hsu, and A. J. Hsueh. 2000. MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain. J. Biol. Chem. 275: 25255–25261.
   PubMed Web of Science ®Google Scholar
• Bingle, C. D., R. W. Craig, B. M. Swales, V. Singleton, P. Zhou, and M. K. Whyte. 2000. Exon skipping in Mcl-1 results in a bcl-2 homology domain 3 only gene product that promotes cell death. J. Biol. Chem. 275: 22136–22146.
   PubMed Web of Science ®Google Scholar
• Boise, L. H., M. Gonzalez-Garcia, C. E. Postema, L. Ding, T. Lindsten, L. A. Turka, X. Mao, G. Nunez, and C. B. Thompson. 1993. bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death. Cell 74: 597–608.
   PubMed Web of Science ®Google Scholar
• Bouillet, P., D. Metcalf, D. C. Huang, D. M. Tarlinton, T. W. Kay, F. Kontgen, J. M. Adams, and A. Strasser. 1999. Proapoptotic Bcl-2 relative Bim required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity. Science 286: 1735–1738.
   PubMed Web of Science ®Google Scholar
• Bouillet, P., L. C. Zhang, D. C. Huang, G. C. Webb, C. D. Bottema, P. Shore, H. J. Eyre, G. R. Sutherland, and J. M. Adams. 2001. Gene structure alternative splicing, and chromosomal localization of pro-apoptotic Bcl-2 relative Bim. Mamm. Genome 12: 163–168.
   PubMed Web of Science ®Google Scholar
• Cuddeback, S. M., H. Yamaguchi, K. Komatsu, T. Miyashita, M. Yamada, C. Wu, S. Singh, and H. G. Wang. 2001. Molecular cloning and characterization of Bif-1. A novel Src homology 3 domain-containing protein that associates with Bax. J. Biol. Chem. 276: 20559–20565.
   PubMed Web of Science ®Google Scholar
• Desagher, S., A. Osen-Sand, A. Nichols, R. Eskes, S. Montessuit, S. Lauper, K. Maundrell, B. Antonsson, and J. C. Martinou. 1999. Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. J. Cell Biol. 144: 891–901.
   PubMed Web of Science ®Google Scholar
• Dijkers, P. F., R. H. Medemadagger, J. W. Lammers, L. Koenderman, and P. J. Coffer. 2000. Expression of the pro-apoptotic Bcl-2 family member Bim is regulated by the forkhead transcription factor FKHR-L1. Curr. Biol. 10: 1201–1204.
   PubMed Web of Science ®Google Scholar
• Gilmore, A. P., A. D. Metcalfe, L. H. Romer, and C. H. Streuli. 2000. Integrin-mediated survival signals regulate the apoptotic function of Bax through its conformation and subcellular localization. J. Cell Biol. 149: 431–446.
   PubMed Web of Science ®Google Scholar
• Griffiths, G. J., B. M. Corfe, P. Savory, S. Leech, M. Degli Esposti, J. S. Hickman, and C. Dive. 2001. Cellular damage signals promote sequential changes at the N-terminus and BH-1 domain of the pro-apoptotic protein Bak. Oncogene 20: 7668–7675.
   PubMed Web of Science ®Google Scholar
• Hsu, Y. T., and R. J. Youle. 1998. Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations. J. Biol. Chem. 273: 10777–10783.
   PubMed Web of Science ®Google Scholar
• Hsu, Y. T., and R. J. Youle. 1997. Nonionic detergents induce dimerization among members of the Bcl-2 family. J. Biol. Chem. 272: 13829–13834.
   PubMed Web of Science ®Google Scholar
• Jiang, Z. H., and J. Y. Wu. 1999. Alternative splicing and programmed cell death. Proc. Soc. Exp. Biol. Med. 220: 64–72.
   PubMed Web of Science ®Google Scholar
• Kataoka, T., N. Holler, O. Micheau, F. Martinon, A. Tinel, K. Hofmann, and J. Tschopp. 2001. Bcl-rambo, a novel Bcl-2 homologue that induces apoptosis via its unique C-terminal extension. J. Biol. Chem. 276: 19548–19554.
   PubMed Web of Science ®Google Scholar
• Kelekar, A., and C. B. Thompson. 1998. Bcl-2-family proteins: the role of the BH3 domain in apoptosis. Trends Cell Biol. 8: 324–330.
   PubMed Web of Science ®Google Scholar
• Makin, G. W., B. M. Corfe, G. J. Griffiths, A. Thistlethwaite, J. A. Hickman, and C. Dive. 2001. Damage-induced Bax N-terminal change, translocation to mitochondria and formation of Bax dimers/complexes occur regardless of cell fate. EMBO J. 20: 6306–6315.
   PubMed Web of Science ®Google Scholar
• Murphy, K. M., U. N. Streips, and R. B. Lock. 2000. Bcl-2 inhibits a Fas-induced conformational change in the Bax N terminus and Bax mitochondrial translocation. J. Biol. Chem. 275: 17225–17228.
   PubMedGoogle Scholar
• Nechushtan, A., C. L. Smith, I. Lamensdorf, S. H. Yoon, and R. J. Youle. 2001. Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis. J. Cell Biol. 153: 1265–1276.
   PubMed Web of Science ®Google Scholar
• O'Connor, L., A. Strasser, L. A. O'Reilly, G. Hausmann, J. M. Adams, S. Cory, and D. C. Huang. 1998. Bim: a novel member of the Bcl-2 family that promotes apoptosis. EMBO J. 17: 384–395.
   PubMed Web of Science ®Google Scholar
• O'Reilly, L. A., L. Cullen, J. Visvader, G. J. Lindeman, C. Print, M. L. Bath, D. C. Huang, and A. Strasser. 2000. The proapoptotic BH3-only protein bim is expressed in hematopoietic, epithelial, neuronal, and germ cells. Am. J. Pathol. 157: 449–461.
   PubMed Web of Science ®Google Scholar
• Perez, D., and E. White. 2000. TNF-alpha signals apoptosis through a bid-dependent conformational change in Bax that is inhibited by E1B 19K. Mol. Cell 6: 53–63.
   PubMed Web of Science ®Google Scholar
• Puig, O., F. Caspary, G. Rigaut, B. Rutz, E. Bouveret, E. Bragado-Nilsson, M. Wilm, and B. Seraphin. 2001. The tandem affinity purification (tap) method: a general procedure of protein complex purification. Methods 24: 218–229.
   PubMed Web of Science ®Google Scholar
• Putcha, G. V., K. L. Moulder, J. P. Golden, P. Bouillet, J. A. Adams, A. Strasser, and E. M. Johnson. 2001. Induction of bim, a proapoptotic bh3-only bcl-2 family member, is critical for neuronal apoptosis. Neuron 29: 615–628.
   PubMed Web of Science ®Google Scholar
• Puthalakath, H., D. C. Huang, L. A. O'Reilly, S. M. King, and A. Strasser. 1999. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol. Cell 3: 287–296.
   PubMed Web of Science ®Google Scholar
• Reed, R. 1989. The organization of 3′ splice-site sequences in mammalian introns. Genes Dev. 3: 2113–2123.
   PubMedGoogle Scholar
• Rigaut, G., A. Shevchenko, B. Rutz, M. Wilm, M. Mann, and B. Seraphin. 1999. A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 17: 1030–1032.
   PubMed Web of Science ®Google Scholar
• Shiraiwa, N., N. Inohara, S. Okada, M. Yuzaki, S. Shoji, and S. Ohta. 1996. An additional form of rat Bcl-x, Bcl-xbeta, generated by an unspliced RNA, promotes apoptosis in promyeloid cells. J. Biol. Chem. 271: 13258–13265.
   PubMedGoogle Scholar
• Stamm, S., M. Q. Zhang, T. G. Marr, and D. M. Helfman. 1994. A sequence compilation and comparison of exons that are alternatively spliced in neurons. Nucleic Acids Res. 22: 1515–1526.
   PubMedGoogle Scholar
• Sun, Y. F., L. Y. Yu, M. Saarma, T. Timmusk, and U. Arumae. 2001. Neuron-specific bcl-2 homology 3 domain-only splice variant of bak is anti-apoptotic in neurons, but pro-apoptotic in non-neuronal cells. J. Biol. Chem. 276: 16240–16247.
   PubMedGoogle Scholar
• Sundararajan, R., and E. White. 2001. E1B 19K blocks Bax oligomerization and tumor necrosis factor alpha-mediated apoptosis. J. Virol. 75: 7506–7516.
   PubMedGoogle Scholar
• Suzuki, M., R. J. Youle, and N. Tjandra. 2000. Structure of Bax: coregulation of dimer formation and intracellular localization. Cell 103: 645–654.
   PubMed Web of Science ®Google Scholar
• Tan, K. O., K. M. Tan, S. L. Chan, K. S. Yee, M. Bevort, K. C. Ang, and V. C. Yu. 2001. MAP-1, a novel proapoptotic protein containing a BH3-like motif that associates with Bax through its Bcl-2 homology domains. J. Biol. Chem. 276: 2802–2807.
   PubMed Web of Science ®Google Scholar
• U, M., T. Miyashita, Y. Shikama, K. Tadokoro, and M. Yamada. 2001. Molecular cloning and characterization of six novel isoforms of human Bim, a member of the proapoptotic Bcl-2 family. FEBS Lett. 509: 135–141.
   PubMedGoogle Scholar
• Wang, K., X. M. Yin, D. T. Chao, C. L. Milliman, and S. J. Korsmeyer. 1996. BID: a novel BH3 domain-only death agonist. Genes Dev. 10: 2859–2869.
   PubMed Web of Science ®Google Scholar
• Wei, M. C., T. Lindsten, V. K. Mootha, S. Weiler, A. Gross, M. Ashiya, C. B. Thompson, and S. J. Korsmeyer. 2000. tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c. Genes Dev. 14: 2060–2071.
   PubMed Web of Science ®Google Scholar
• Wei, M. C., W. X. Zong, E. H. Cheng, T. Lindsten, V. Panoutsakopoulou, A. J. Ross, K. A. Roth, G. R. MacGregor, C. B. Thompson, and S. J. Korsmeyer. 2001. Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science 292: 727–730.
   PubMed Web of Science ®Google Scholar
• Zong, W. X., T. Lindsten, A. J. Ross, G. R. MacGregor, and C. B. Thompson. 2001. BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. Genes Dev. 15: 1481–1486.
   PubMed Web of Science ®Google Scholar