Mitochondrial ROS - radical detoxification, mediated by protein kinase D

Trends in Cell Biology

Volumn 17, Issue 1, 2007, Pages 13-18

  Storz, Peter ^a  

^a MAYO CLINIC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT; OXYGEN RADICAL; PROTEIN KINASE D; PROTEIN SERINE THREONINE KINASE; REACTIVE OXYGEN METABOLITE;

AGING; ANTIOXIDANT ACTIVITY; ARTICLE; CELL ACTIVITY; CELL DAMAGE; CELL DEATH; CELL NUCLEUS; CELL ORGANELLE; CELL PROTECTION; CELL SURVIVAL; CYTOTOXICITY; DISORDERS OF MITOCHONDRIAL FUNCTIONS; ENZYME ACTIVATION; FUNCTIONAL PROTEOMICS; GENE; GENE FUNCTION; GENE INDUCTION; HUMAN; LIFESPAN; MITOCHONDRIAL RESPIRATION; MOLECULAR MODEL; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN FUNCTION; RESPIRATORY CHAIN; SIGNAL TRANSDUCTION;

1-PHOSPHATIDYLINOSITOL 3-KINASE; ANIMALS; ANTIOXIDANTS; CELL DEATH; CELL NUCLEUS; ELECTRON TRANSPORT; FREE RADICALS; HUMANS; MITOCHONDRIA; MODELS, BIOLOGICAL; OXIDATIVE STRESS; OXYGEN; PROTEIN KINASE C; REACTIVE OXYGEN SPECIES; SIGNAL TRANSDUCTION;

EID: 33845953689     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2006.11.003     Document Type: Article

References (51)

1. Finkel T. Opinion: Radical medicine: treating ageing to cure disease. Nat Rev Mol Cell Biol 6 (2005) 971-976
2. Storz P. Reactive oxygen species in tumor progression. Front. Biosci. 10 (2005) 1881-1896
3. Cadenas E. Mitochondrial free radical production and cell signaling. Mol. Aspects Med. 25 (2004) 17-26
4. Choi W.S., et al. Phosphorylation of p38 MAPK induced by oxidative stress is linked to activation of both caspase-8- and -9-mediated apoptotic pathways in dopaminergic neurons. J. Biol. Chem. 279 (2004) 20451-20460
5. Storz P., et al. Protein kinase D mediates mitochondrion-to-nucleus signaling and detoxification from mitochondrial reactive oxygen species. Mol. Cell. Biol. 25 (2005) 8520-8530
6. Storz P., and Toker A. Protein kinase D mediates a stress-induced NF-κB activation and survival pathway. EMBO J. 22 (2003) 109-120
7. Datta S.R., et al. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 91 (1997) 231-241
8. Song J., et al. Protein kinase D protects against oxidative stress-induced intestinal epithelial cell injury via Rho/ROK/PKC-δ pathway activation. Am J Physiol Cell Physiol 290 (2006) C1469-C1476
9. Storz P., et al. Protein kinase Cδ selectively regulates protein kinase D-dependent activation of NF-κB in oxidative stress signaling. Mol. Cell. Biol. 24 (2004) 2614-2626
10. Storz P., and Toker A. NF-κB signaling - an alternate pathway for oxidative stress responses. Cell Cycle 2 (2003) 9-10
11. Han D., et al. Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space. Biochem. J. 353 (2001) 411-416
12. Yankovskaya V., et al. Architecture of succinate dehydrogenaseand reactive oxygen species generation. Science 299 (2003) 700-704
13. Johnson F., and Giulivi C. Superoxide dismutases and their impact upon human health. Mol. Aspects Med. 26 (2005) 340-352
14. Crompton M. The mitochondrial permeability transition pore and its role in cell death. Biochem. J. 341 (1999) 233-249
15. 2: regulation of peroxiredoxin, catalase, and glutathione peroxidase via post-translational modification. Antioxid. Redox Signal. 7 (2005) 619-626
16. Storz P. Reactive oxygen species-mediated mitochondria-to-nucleus signaling: a key to aging and radical-caused diseases. Sci. STKE 2006 (2006) re3
17. Tonks N.K. Redox redux: revisiting PTPs and the control of cell signaling. Cell 121 (2005) 667-670
18. Manning G., et al. The protein kinase complement of the human genome. Science 298 (2002) 1912-1934
19. Auer A., et al. Role of the regulatory domain of protein kinase D2 in phorbol ester binding, catalytic activity, and nucleocytoplasmic shuttling. Mol. Biol. Cell 16 (2005) 4375-4385
20. Hausser A., et al. Protein kinase D regulates vesivular transport by phosphorylating and activating phosphatidylinositol-4 kinase IIIbeta at the Golgi complex. Nat. Cell Biol. 7 (2005) 880-886
21. Rozengurt E., et al. Protein kinase D signaling. J. Biol. Chem. 280 (2005) 13205-13208
22. Yeaman C., et al. Protein kinase D regulates basolateral membrane protein exit from trans-Golgi network. Nat. Cell Biol. 6 (2004) 106-112
23. Van Lint J., et al. Protein kinase D: an intracellular traffic regulator on the move. Trends Cell Biol. 12 (2002) 193-200
24. Storz P., et al. Tyrosine phosphorylation of protein kinase D in the pleckstrin homology domain leads to activation. J. Biol. Chem. 278 (2003) 17969-17976
25. Wang Q.J., et al. PKD at the crossroads of DAG and PKC signaling. Trends Pharmacol. Sci. 27 (2006) 317-323
26. Storz P., et al. Activation loop phosphorylation controls protein kinase D-dependent activation of nuclear factor κB. Mol. Pharmacol. 66 (2004) 870-879
27. Yang C., and Kazanietz M.G. Divergence and complexities in DAG signaling: looking beyond PKC. Trends Pharmacol. Sci. 24 (2003) 602-608
28. Itoh S., et al. Mitochondrial Dok-4 recruits Src kinase and regulates NF-kappaB activation in endothelial cells. J. Biol. Chem. 280 (2005) 26384-26396
29. Soltys B.J., et al. Localization of P32 protein (gC1q-R) in mitochondria and at specific extramitochondrial locations in normal tissues. Histochem. Cell Biol. 114 (2000) 245-255
30. Jiang J., et al. Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 3572-3577
31. Robles-Flores M., et al. p32 (gC1qBP) is a general protein kinase C (PKC)-binding protein; interaction and cellular localization of P32-PKC complexes in rat hepatocytes. J. Biol. Chem. 277 (2002) 5247-5255
32. Storz P., et al. Protein kinase C [micro] is regulated by the multifunctional chaperon protein p32. J. Biol. Chem. 275 (2000) 24601-24607
33. Carnegie G.K., et al. AKAP-Lbc nucleates a protein kinase D activation scaffold. Mol. Cell 15 (2004) 889-899
34. Karin M. Nuclear factor-kappaB in cancer development and progression. Nature 441 (2006) 431-436
35. Yamamoto Y., and Gaynor R.B. IκB kinases: key regulators of the NF-κB pathway. Trends Biochem. Sci. 29 (2004) 72-79
36. + human myeloid leukemia cells. Cancer Res. 64 (2004) 8939-8944
37. Imbert V., et al. Tyrosine phosphorylation of I kappa B-alpha activates NF-kappa B without proteolytic degradation of I kappa B-alpha. Cell 86 (1996) 787-798
38. Beraud C., et al. Involvement of regulatory and catalytic subunits of phosphoinositide 3-kinase in NF-kappaB activation. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 429-434
39. Doppler H., et al. A phosphorylation state-specific antibody recognizes Hsp27, a novel substrate of protein kinase D. J. Biol. Chem. 280 (2005) 15013-15019
40. Park K.J., et al. Heat shock protein 27 association with the IκB kinase complex regulates tumor necrosis factor α-induced NF-κ B activation. J. Biol. Chem. 278 (2003) 35272-35278
41. Storz P., et al. Functional dichotomy of A20 in apoptotic and necrotic cell death. Biochem. J. 387 (2005) 47-55
42. Heyninck K., and Beyaert R. A20 inhibits NF-κB activation by dual ubiquitin-editing functions. Trends Biochem. Sci. 30 (2005) 1-4
43. Ghafourifar P., and Cadenas E. Mitochondrial nitric oxide synthase. Trends Pharmacol. Sci. 26 (2005) 190-195
44. Hurd C., et al. Protein kinase D complexes with C-Jun N-terminal kinase via activation loop phosphorylation and phosphorylates the C-Jun N-terminus. Oncogene 21 (2002) 2154-2160
45. Hurd C., and Rozengurt E. Protein kinase D is sufficient to suppress EGF-induced c-Jun Ser 63 phosphorylation. Biochem. Biophys. Res. Commun. 282 (2001) 404-408
46. Harman D. Role of free radicals in aging and disease. Ann. N. Y. Acad. Sci. 673 (1992) 126-141
47. Beal M.F. Mitochondria, oxidative damage, and inflammation in Parkinson's disease. Ann. N. Y. Acad. Sci. 991 (2003) 120-131
48. Madamanchi N.R., et al. Oxidative stress and vascular disease. Arterioscler. Thromb. Vasc. Biol. 25 (2005) 29-38
49. Jackson J.H. Potential molecular mechanisms of oxidant-induced carcinogenesis. Environ. Health Perspect. 102 Suppl. 10 (1994) 155-157
50. Imlay J.A., et al. Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro. Science 240 (1988) 640-642
51. Mello Filho A.C., and Meneghini R. In vivo formation of single-strand breaks in DNA by hydrogen peroxide is mediated by the Haber-Weiss reaction. Biochim. Biophys. Acta 781 (1984) 56-63