The endoplasmic reticulum gateway to apoptosis by Bcl-XL modulation of the InsP3R (original) (raw)

References

  1. Wei, M. C. et al. Proapoptotic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death. Science 292, 727–730 (2001).
    Article CAS Google Scholar
  2. Vander Heiden, M. G. & Thompson, C. B. Bcl-2 proteins: regulators of apoptosis or of mitochondrial homeostasis? Nature Cell Biol. 1, E209–E216 (1999).
    Article CAS Google Scholar
  3. Krajewski, S. et al. Investigation 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).
    CAS PubMed Google Scholar
  4. Distelhorst, C. W. & Shore, G. C. Bcl-2 and calcium: controversy beneath the surface. Oncogene 23, 2875–2880 (2004).
    Article CAS Google Scholar
  5. Jurgensmeier, J. M. et al. Bax directly induces release of cytochrome c from isolated mitochondria. Proc. Natl Acad. Sci. USA 95, 4997–5002 (1998).
    Article CAS Google Scholar
  6. Antonsson, B. et al. Inhibition of Bax channel-forming activity by Bcl-2. Science 277, 370–372 (1997).
    Article CAS Google Scholar
  7. Zong, W. X. et al. Bax and Bak can localize to the endoplasmic reticulum to initiate apoptosis. J. Cell Biol. 162, 59–69 (2003).
    Article CAS Google Scholar
  8. Breckenridge, D. G., Germain, M., Mathai, J. P., Nguyen, M. & Shore, G. C. Regulation of apoptosis by endoplasmic reticulum pathways. Oncogene 22, 8608–8618 (2003).
    Article CAS Google Scholar
  9. Orrenius, S., Zhivotovsky, B. & Nicotera, P. Regulation of cell death: the calcium-apoptosis link. Nature Rev. Mol. Cell Biol. 4, 552–565 (2003).
    Article CAS Google Scholar
  10. Scorrano, L. et al. BAX and BAK regulation of endoplasmic reticulum Ca2+: A control point for apoptosis. Science 300, 135–139 (2003).
    Article CAS Google Scholar
  11. Rizzuto, R. et al. Calcium and apoptosis: facts and hypotheses. Oncogene 22, 8619–8627 (2003).
    Article CAS Google Scholar
  12. Duchen, M. R. Mitochondria and calcium: from cell signalling to cell death. J. Physiol. 529, 57–68 (2000).
    Article CAS Google Scholar
  13. Nakagawa, T. & Yuan, J. Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. J. Cell Biol. 150, 887–894 (2000).
    Article CAS Google Scholar
  14. Szalai, G., Krishnamurthy, R. & Hajnoczky, G. Apoptosis driven by IP3-linked mitochondrial calcium signals. EMBO J. 18, 6349–6361 (1999).
    Article CAS Google Scholar
  15. Oakes, S. A. et al. Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum. Proc. Natl Acad. Sci. USA 102, 105–110 (2005).
    Article CAS Google Scholar
  16. Chen, R. et al. Bcl-2 functionally interacts with inositol 1,4,5-trisphosphate receptors to regulate calcium release from the ER in response to inositol 1,4,5-trisphosphate. J. Cell Biol. 166, 193–203 (2004).
    Article CAS Google Scholar
  17. Mak, D. O., McBride, S. & Foskett, J. K. Inositol 1,4,5-trisphosphate activation of inositol trisphosphate receptor Ca2+ channel by ligand tuning of Ca2+ inhibition. Proc. Natl Acad. Sci. USA 95, 15821–15825 (1998).
    Article CAS Google Scholar
  18. Luzzi, V., Sims, C. E., Soughayer, J. S. & Allbritton, N. L. The physiologic concentration of inositol 1,4,5-trisphosphate in the oocytes of Xenopus laevis. J. Biol. Chem. 273, 28657–28662 (1998).
    Article CAS Google Scholar
  19. Korsmeyer, S. J. et al. Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c. Cell Death Differ. 7, 1166–1173 (2000).
    Article CAS Google Scholar
  20. Minn, A. J. et al. Bcl-xL forms an ion channel in synthetic lipid membranes. Nature 385, 353–357 (1997).
    Article CAS Google Scholar
  21. Sugawara, H., Kurosaki, M., Takata, M. & Kurosaki, T. Genetic evidence for involvement of type 1, type 2 and type 3 inositol 1,4,5-trisphosphate receptors in signal transduction through the B-cell antigen receptor. EMBO J. 16, 3078–3088 (1997).
    Article CAS Google Scholar
  22. Foyouzi-Youssefi, R. et al. Bcl-2 decreases the free Ca2+ concentration within the endoplasmic reticulum. Proc. Natl Acad. Sci. USA 97, 5723–5728 (2000).
    Article CAS Google Scholar
  23. Palmer, A. E., Jin, C., Reed, J. C. & Tsien, R. Y. Bcl-2-mediated alterations in endoplasmic reticulum Ca2+ analyzed with an improved genetically encoded fluorescent sensor. Proc. Natl Acad. Sci. USA 101, 17404–17409 (2004).
    Article CAS Google Scholar
  24. Pinton, P. et al. Reduced loading of intracellular Ca2+ stores and downregulation of capacitative Ca2+ influx in Bcl-2-overexpressing cells. J. Cell Biol. 148, 857–862 (2000).
    Article CAS Google Scholar
  25. Niiro, H. & Clark, E. A. Regulation of B-cell fate by antigen-receptor signals. Nature Rev. Immunol. 2, 945–956 (2002).
    Article CAS Google Scholar
  26. Doi, T., Motoyama, N., Tokunaga, A. & Watanabe, T. Death signals from the B cell antigen receptor target mitochondria, activating necrotic and apoptotic death cascades in a murine B cell line, WEHI-231. Int. Immunol. 11, 933–941 (1999).
    Article CAS Google Scholar
  27. Hajnoczky, G., Robb-Gaspers, L. D., Seitz, M. B. & Thomas, A. P. Decoding of cytosolic calcium oscillations in the mitochondria. Cell 82, 415–424 (1995).
  28. Kowaltowski, A. J. & Fiskum, G. Redox mechanisms of cytoprotection by Bcl-2. Antioxid. Redox. Signal. 7, 508–514 (2005).
    Article CAS Google Scholar
  29. Hammerman, P. S., Fox, C. J. & Thompson, C. B. Beginnings of a signal-transduction pathway for bioenergetic control of cell survival. Trends Biochem. Sci. 29, 586–592 (2004).
    Article CAS Google Scholar
  30. Plas, D. R. & Thompson, C. B. Cell metabolism in the regulation of programmed cell death. Trends Endocrinol. Metab. 13, 75–78 (2002).
    Article Google Scholar
  31. Shimizu, H., Borin, M. L. & Blaustein, M. P. Use of La3+ to distinguish activity of the plasmalemmal Ca2+ pump from Na+/Ca2+ exchange in arterial myocytes. Cell Calcium 21, 31–41 (1997).
    Article CAS Google Scholar
  32. Haynes, L. P., Tepikin, A. V. & Burgoyne, R. D. Calcium-binding protein 1 is an inhibitor of agonist-evoked, inositol 1,4,5-trisphosphate-mediated calcium signaling. J. Biol. Chem. 279, 547–555 (2004).
    Article CAS Google Scholar

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