Phosphorylation and inactivation of BAD by mitochondria-anchored protein kinase A

Molecular Cell

Volumn 3, Issue 4, 1999, Pages 413-422

  Harada, Hisashi ^a,b   Becknell, Brian ^a   Wilm, Matthias ^d   Mann, Matthias ^d   Huang, Lily Jun shen ^e   Taylor, Susan S ^e   Scott, John D ^c   Korsmeyer, Stanley J ^a,b  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b DANA FARBER CANCER INSTITUTE   (United States)

^c OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^d EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^e UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; PROTEIN BCL 2; PROTEIN KINASE; PROTEIN KINASE (CALCIUM,CALMODULIN) II; PROTEIN SERINE KINASE;

ARTICLE; CELL DEATH; CELL SURVIVAL; ENZYME ACTIVITY; ENZYME PURIFICATION; MITOCHONDRION; NONHUMAN; PHOSPHORYLATION; PROTEIN FAMILY; PROTEIN INTERACTION;

EID: 0033120591     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(00)80469-4     Document Type: Article

References (54)

1. Alessi, D.R., Cuenda, A., Cohen, P., Dudley, D.T., and Saltiel, A.R. (1995). PD 098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo. J. Biol. Chem. 270, 27489-27494.
2. Andjelkovic, M., Alessi, D.R., Meier, R., Fernandez, A., Lamb, N.J., Frech, M., Cron, P., Cohen, P., Lucocq, J.M., and Hemmings, B.A. (1997). Role of translocation in the activation and function of protein kinase B. J. Biol. Chem. 272, 31515-31524.
3. Berridge, M.V., Tan, A.S., and Hilton, C.J. (1993). Cyclic adenosine monophosphate promotes cell survival and retards apoptosis in a factor-dependent bone marrow-derived cell line. Exp. Hematol. 21, 269-276.
4. Blume-Jensen, P., Janknecht, R., and Hunter, T. (1998). The kit receptor promotes cell survival via activation of Pl 3-kinase and subsequent Akt-mediated phosphorylation of bad on Ser136. Curr. Biol. 8, 779-782.
5. Boyd, J.M., Gallo, G.J., Elangovan, B., Houghton, A.B., Malstrom, S., Avery, B.J., Ebb, R.G., Subramanian, T., Chittenden, T., Lutz, R.J., and Chinnadurai, G. (1995). Bik, a novel death-inducing protein shares a distinct sequence motif with Bcl-2 family proteins and interacts with viral and cellular survival-promoting proteins. Oncogene 11, 1921-1928.
6. Carr, D.W., Hausken, Z.E., Fraser, I.D.C., Stofko-Hahn, R.E., and Scott, J.D. (1992). Association of the type II cAMP-dependent protein kinase with a human thyroid RII-anchoring protein. J. Biol. Chem. 267, 13376-13382.
7. Coleman, D.L., Liu, J., and Bartiss, A.H. (1989). Recombinant granulocyte-macrophage colony-stimulating factor increases adenylate cyclase activity in murine peritoneal macrophages. J. Immunol. 143, 4134-4140.
8. Conradt, B., and Horvitz, H.R. (1998). The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9. Cell 93, 519-529.
9. Datta, S.R., Dudek, H., Tao, X., Masters, S., Fu, H., Gotoh, Y., and Greenberg, M.E. (1997). Akt phosphorylation of bad couples survival signals to the cell-intrinsic death machinery. Cell 91, 231-241.
10. de Jong, D., Prins, F.A., Mason, D.Y., Reed, J.C., van Ommen, G.N., and P.M. Kluin. (1994). Subcellular localization of the Bcl-2 protein in malignant and normal lymphoid cells. Cancer Res. 54, 256.
11. del Peso, L., Gonzalez-Garcia, M., Page, C., Herrera, R., and Nunez, G. (1997). Interleukin-3-induced phosphorylation of bad through the protein kinase Akt. Science 278, 687-689.
12. Dell'Acqua, M.L., and Scott, J.D. (1997). Protein kinase A anchoring. J. Biol. Chem. 272, 12881-12884.
13. Franke, T.F., Yang, S., Chan, T.O., Datta, K., Kazlauskas, A., Morrison, D.K., Kaplan, D.R., and Tsichlis, P.N. (1995). The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell 81, 727-736.
14. Franke, T.F., Kaplan, D.R., and Cantley, L.C. (1997). PI3K: Downstream AKTion blocks apoptosis. Cell 88, 435-437.
15. Gross, A., Jockel, J., Wei, M.C., and Korsmeyer, S.J. (1998). Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis. EMBO J. 17, 3878-3885.
16. L prevents this release but not tumor necrosis factor-R1/Fas death. J. Biol. Chem. 274, 1156-1163.
17. L, is a potent death agonist. J. Biol. Chem. 272, 12881-12884.
18. Hockenbery, D., 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.
19. Huang, L.J., Durick, K., Weiner, J.A., Chun, J., and Taylor, S.S. (1997). Identification of a novel protein kinase A anchoring protein that binds both type I and type II regulatory subunits. J. Biol. Chem. 272, 8057-8064.
20. Hubbard, M.J., and Cohen, P. (1993). On target with a new mechanism for the regulation of protein phosphorylation. Trends Biochem. Sci. 18, 172-177.
21. Ihle, J.N. (1995). Cytokine receptor signaling. Nature 377, 591-594.
22. L. EMBO J. 16, 1686-1694.
23. L. Mol. Cell. Biol. 17, 7040-7046.
24. Kroemer, G., Zamzami, N., and Susin, S.A. (1997). Mitochondrial control of apoptosis. Immunol. Today 18, 44-51.
25. Lester, L.B., Langeberg, L.K., and Scott, J.D. (1997). Anchoring of protein kinase A facilitates hormone-mediated insulin secretion. Proc. Natl. Acad. Sci. USA. 94, 14942-14947.
26. Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S.M., Ahmad, M., Alnemri, E.S., Wang, X. (1997). Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91, 479-489.
27. Li, H., Zhu, H., Xu, C.J., and Yuan, J. (1998). Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 94, 491-501.
28. Lin, R.-Y., Moss, S.B., and Rubin, C.S. (1995). Characterization of S-AKAP84, a novel developmentally regulated kinase anchor protein of male germ cells. J. Biol. Chem. 17, 27804-27811.
29. Luo, X., Budihardjo, I., Zou, H., Slaughter, C., and Wang, X. (1998). Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 94, 481-490.
30. McDonnell, J.M., Fushman, D., Milliman, C.L., Korsmeyer, S.J., and Cowburn, D. (1999). Solution structure of the proapoptotic molecule, BID: A structural basis for apoptotic agonists and antagonists. Cell 96, 625-634.
31. Meyer-Franke, A., Kaplan, M.R., Pfrieger, F.W., and Barres, B.A. (1995). Characterization of the signaling interactions that promote the survival and growth of developing retinal ganglion cells in culture. Neuron 15, 805-819.
32. Miyajima, A., Mui, A.L., Ogorochi, T., and Sakamaki, K. (1993). Receptors for granulocyte-macrophage colony-stimulating factor, interleukin-3, and interleukin-5. Blood 82, 1960-1974.
33. Mochly-Rosen, D. (1995). Localization of protein kinases by anchoring proteins: A theme in signal transduction. Science 268, 247-251.
34. Nguyen, M., Millar, D.G., Yong, V.W., Korsmeyer, S.J., and Shore, G.C. (1993). Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence. J. Biol. Chem. 268, 25265-25268.
35. O'Connor, L., Strasser, A., O'Reilly, L.A., Hausmann, G., Adams, J.M., Cory, S., and Huang, D.C.S. (1998). Bim: A novel member of the Bcl-2 family that promotes apoptosis. EMBO J. 17, 384-395.
36. Oltvai, 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.
37. Ottilie, S., Diaz, J.L., Horne, W., Chang, J., Wang, Y., Wilson, G., Chang, S., Weeks, S., Fritz, L.C., and Oltersdorf, T. (1997). Dimerization properties of human BAD. J. Biol. Chem. 272, 30866-30872.
38. Pastorino, U., Chen, S.T., Tafani, M., Snyder, J.W., and Farber, J.L. (1998). The overexpression of bax produces cell death upon induction of the mitochondrial permeability transition. J. Biol. Chem. 273, 7770-7775.
39. Pawson, T., and Scott, J.D. (1997). Signaling through scaffold, anchoring and adaptor proteins. Science. 278, 2075-2080.
40. Raff, M.C. (1992). Social controls on cell survival and death: An extreme view. Nature 356, 397-400.
41. Rosenmund, C., Carr, D.W., Bergeson, S.E., Nilaver, G., Scott, J.D., and Westbrook, G.L. (1994). Anchoring of protein kinase A is required for modulation of AMPA/kainate receptors on hippocampal neurons. Nature 368, 853-856.
42. L-Bak peptide complex: Recognition between regulators of apoptosis. Science 275, 983-986.
43. Scheid, M.P., and Duronio, V. (1998). Dissociation of cytokine-induced phosphorylation of bad and activation of PKB/akt: Involvement of MEK upstream of bad phosphorylation. Proc. Natl. Acad. Sci. USA 95, 7439-7444.
44. Songyang, Z., Baltimore, D., Cantley, L., Kaplan, D.R., and Franke, T.F. (1997). Interleukin 3-dependent survival by the AKT protein kinase. Proc. Natl. Acad. Sci. USA 94, 11345-11350.
45. L regulates the membrane potential and volume homeostasis of mitochondria. Cell 91, 627-637.
46. Vlahos, C.J., Matter, W.F., Hui, K.Y., and Brown, R.F. (1994). A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8- Phenyl-4H-1-benzopyran-4-one (LY294002). J. Biol. Chem. 269, 5241-5248.
47. von Knethen, A., Lotero, A., and Brune, B. (1998). Etoposide and cisplatin induced apoptosis in activated RAW 264.7 macrophages is attentuated by cAMP-induced gene expression. Oncogene 16, 387-394.
48. Wang H., Rapp, U.R., and Reed, J.C. (1996a). Bcl-2 targets the protein kinase Raf-1 to mitochondria. Cell 87, 629-638.
49. Wang, K., Yin, X.-M., Chao, D.T., Milliman, C.L., and Korsmeyer, S.J. (1996b). BID: A novel BH3 domain-only death agonist. Genes Dev. 10, 2859-2869.
50. Wolter, K.G., Hsu, Y.T., Smith, C.L., Nechushtan, A., Xi, X.G., and Youle, R.J. (1997). Movement of bax from the cytosol to mitochondria during apoptosis. J. Cell Biol. 139, 1281-1292.
51. Xiang, J., Chao, D.T., and Korsmeyer, S.J. (1996). Bax-induced cell death may not require interleukin 1 beta-converting enzyme-like proteases. Proc. Natl. Acad. Sci. USA 93, 14559-14563.
52. L and Bcl-2 displaces bax and promotes cell death. Cell 80, 285-291.
53. L. Cell 87, 619-628.
54. L and pro-apoptotic activity. J. Biol. Chem. 272, 24101-24104.