The endoplasmic reticulum gateway to apoptosis by Bcl-XL modulation of the InsP3R

Nature Cell Biology

Volumn 7, Issue 10, 2005, Pages 1021-1028

  White, Carl ^a   Li, Chi ^a   Yang, Jun ^a   Petrenko, Nataliya B ^a   Madesh, Muniswamy ^a,b   Thompson, Craig B ^a   Foskett, J Kevin ^a,c  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL XL;

ANIMAL CELL; APOPTOSIS; ARTICLE; BIOCHEMISTRY; BIOENERGY; CALCIUM TRANSPORT; CARBOXY TERMINAL SEQUENCE; CELL MEMBRANE; CELL PROTECTION; CELL SURVIVAL; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; EXTRACELLULAR CALCIUM; IN VITRO STUDY; IN VIVO STUDY; MITOCHONDRION; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM; SENSITIVITY ANALYSIS; SIGNAL TRANSDUCTION;

APOPTOSIS; BCL-X PROTEIN; CALCIUM CHANNELS; CALCIUM SIGNALING; CELL LINE; CELL MEMBRANE; ENDOPLASMIC RETICULUM; HUMANS; INOSITOL 1,4,5-TRISPHOSPHATE RECEPTORS; RECEPTORS, CYTOPLASMIC AND NUCLEAR; TIME FACTORS;

EID: 27144487808     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1302     Document Type: Article

References (32)

1. Wei, M. C. et al. Proapoptotic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death. Science 292, 727-730 (2001).
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).
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).
4. Distelhorst, C. W. & Shore, G. C. Bcl-2 and calcium: Controversy beneath the surface. Oncogene 23, 2875-2880 (2004).
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).
6. Antonsson, B. et al. Inhibition of Bax channel-forming activity by Bcl-2. Science 277, 370-372 (1997).
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).
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).
9. Orrenius, S., Zhivotovsky, B. & Nicotera, P. Regulation of cell death: the calcium-apoptosis link. Nature Rev. Mol. Cell Biol. 4, 552-565 (2003).
10. 2+: A control point for apoptosis. Science 300, 135-139 (2003).
11. Rizzuto, R. et al. Calcium and apoptosis: Facts and hypotheses. Oncogene 22, 8619-8627 (2003).
12. Duchen, M. R. Mitochondria and calcium: From cell signalling to cell death. J. Physiol. 529, 57-68 (2000).
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).
14. 3-linked mitochondrial calcium signals. EMBO J. 18, 6349-6361 (1999).
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).
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).
17. 2+ inhibition. Proc. Natl Acad. Sci. USA 95, 15821-15825 (1998).
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).
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).
20. L forms an ion channel in synthetic lipid membranes. Nature 385, 353-357 (1997).
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).
22. 2+ concentration within the endoplasmic reticulum. Proc. Natl Acad. Sci. USA 97, 5723-5728 (2000).
23. 2+ analyzed with an improved genetically encoded fluorescent sensor. Proc. Natl Acad. Sci. USA 101, 17404-17409 (2004).
24. 2+ influx in Bcl-2-overexpressing cells. J. Cell Biol. 148, 857-862 (2000).
25. Niiro, H. & Clark, E. A. Regulation of B-cell fate by antigen-receptor signals. Nature Rev. Immunol. 2, 945-956 (2002).
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).
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).
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).
30. Plas, D. R. & Thompson, C. B. Cell metabolism in the regulation of programmed cell death. Trends Endocrinol. Metab. 13, 75-78 (2002).
31. 2+ exchange in arterial myocytes. Cell Calcium 21, 31-41 (1997).
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).