Bcl-2 and Bax interactions in mitochondria probed with green fluorescent protein and fluorescence resonance energy transfer (original) (raw)

References

  1. Tsujimoto, Y. and Croce, C.M. 1986. Analysis of the structure, transcripts and protein products of bcl-2, the gene involved in human follicular lymphoma. Proc. Natl. Acad. Sci. USA 83: 5214–5218 .
    Article CAS Google Scholar
  2. Rampino, N., Yamamoto, H. lonov, Y., Li, Y., Sawai, H., Reed, J.C. and Perucho, M. 1997. Somatic frameshifl mutations in the BAX gene in colon cancers of the microsatellite mutator phenotype. Science 275: 967–969.
    Article CAS Google Scholar
  3. Yin, C., Knudson, M.C., Korsymeyer, S.J., and Dyke, T.V. 1997. Bax suppresses tumorigenesis and stimulates apoptosis in vivo. Nature 385: 637–640.
    Article CAS Google Scholar
  4. Hockenbery, D.M., Nunez, G., Milliman, C., Schreiber, R.D., and Korsmeyer, S.J. 1990. Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death. Nature 348: 334–336.
    Article CAS Google Scholar
  5. Oltavi, Z.N., Milliman, C.L. and Korsmeyer, S.J. 1993. Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell 74: 609–619.
    Article Google Scholar
  6. Oltavi, Z.N. and Korsmeyer, S.J. 1994. Checkpoints of dueling dimers foil death wishes Cell 79: 189–192.
    Article Google Scholar
  7. Xiang, J., Chao, D.T. and Korsmeyer, S.J. 1996. BAX-induced cell death may not require interleukin 1B-converting enzyme-like proteases. Proc. Natl. Acad. Sci. USA 93: 14599–14563.
    Google Scholar
  8. Liu, X., Kim, C.N.J., Jemmerson, R. and Wang, X. 1996. Induction of apoptotic program in cell-free extracts: requirement of dATP and cytochrome c. Cell 83: 147–157.
    Article Google Scholar
  9. Chinnaiyan, A.M., O'Rouke, K., Lane, B.R. and Dixit, V.M. 1997. Interaction of CED-4 with CED-3 and CED-9: A molecular framework for cell death. Science 275: 1122–1126.
    Article CAS Google Scholar
  10. Wu, D., Wallen, H.D. and Nunez, G. 1997. Interaction and regulation of subcel-lular localization of CED-4 by CED-9 Science 275: 1126–1129.
    Article CAS Google Scholar
  11. Yang, J., Liu, X., Bhalla, K., Kim, C.N., Ibrado, A.M., Cai, J. et al. 1997. Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked. Science 275: 1129–1132.
    Article CAS Google Scholar
  12. Knudson, M.C. and Korsmeyer, S.J. 1997. Bcl-2 and Bax functions independently to regulate cell death. Nat. Genet. 16, 358–363.
    Article CAS Google Scholar
  13. Reed, J.C., Zha, H., Aime-Sempe, C., Takayama S. and Wang, H. 1996. Structure-function analysis of Bcl-2 family proteins, pp 99–112 in Mechanisms of lymphocyte activation and immune regulation VI. Gupta and Cohen (eds.). Plenum Press, New York.
    Chapter Google Scholar
  14. Cubitt, A.B., Heim, R., Adams, S.R., Boyd, A.E., Gross, L.A. and Tsien, R.Y. 1995. Understanding, improving and using green fluorescent proteins Trends in Biochemical Sciences 20: 448–455.
    Article CAS Google Scholar
  15. Rizzuto, R., Brini, M., De Giorgi, F., Rossi, R., Heim, R., Tsien, R.Y., and Pozzan, T. 1996. Double labeling of subcellular structures with organelle-targeted GFP mutants in vivo. Curr. Biol. 6: 183–188.
    Article CAS Google Scholar
  16. Heim, R., Cubitt, A.B. and Tsien, R.Y. 1995. Improved green fluorescence. Nature 373: 663–664.
    Article CAS Google Scholar
  17. Heim, R. and Tsien, R.Y. 1996. Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer Curr. Biol. 6: 178–182.
    Article CAS Google Scholar
  18. Mitra, R.D., Silva, C.M., and Youvan, D.C. 1996. Fluorescence resonance energy transfers between blue-emitting and red-shifted excitation derivatives of the green fluorescent protein. Gene 1731 3–17.
    Article Google Scholar
  19. Miyawaki, A., Llopis, J., Heim, R., McCaffery, J.M., Adams, J.A., Ikura, M. and Tsien, R.Y. 1997. Fluorescence indicators for Ca2+ based on green fluorescent proteins and calmodulin. Nature 388: 882–887.
    Article CAS Google Scholar
  20. Gonsalez, D.H. and Neupert, W. 1990. Biogenesis of mitochondrial c-type cytochromes. J. Bioenerg. Biomembr. 22: 753–768.
    Google Scholar
  21. Hoppe-Seyler, F. and Butz, K. 1993. Repression of endogenous p53 transactivation function in Hela cervical carcinoma cells by human papillomavirus type 16 E6, human mdm-2 and mutant p53. J. Virol. 67: 3111–3117.
    CAS PubMed PubMed Central Google Scholar
  22. Brown, J., Higo, H., McKalip, A. and Herman, B. 1997. Human papillomavirus (HPV) 16 E6 sensitizes cells to stractyloside-induced spoptosis: role of p53, ICE-like proteases and the mitochondrial permeability transition. J. Cell. Biochem. 66: 245–255.
    Article CAS Google Scholar
  23. Casciola-Rosen, L.A., Nicholson, D.W., Chong, T., Rowan, K.R., Thornberry, N.A., Miller, D.K., and Rosen, A. 1996. Apopain/CPP32 cleaves proteins that are essential for cellular repair, a fundamental principle of apoptotic cell death. J. Exp. Med. 183: 1957–1964.
    Article CAS Google Scholar
  24. Gordon, G.W., Berry, G., Liang, X.H., Levine, B. and Herman, B. 1998. Quantitative fluorescence resonance energy transfer (FRET) measurements using fluorescence microscopy. Biophysical Journal In press.
    Google Scholar
  25. Terry, B.R., Matthews, E.K. and Haseloff, J. 1995. Molecular characterization of recombinant green fluorescent protein by fluorescence correlation microscopy. Biochem. Biophys. Res. Commun. 217 21–27.
    Article CAS Google Scholar
  26. Kharbanda, S., Pandey, P., Schofield, L., Israels, S., Roncinske, R., Yoshida, K. et al. 1997. Role of Bcl-XL as an inhibitor of cytosolic cytochrome c accumulation in DNA damage-induced apoptosis. Proc. Natl. Acad. Sci. USA 94: 6939–6942.
    Article CAS Google Scholar

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