CK2 is the regulator of SIRT1 substrate-binding affinity, deacetylase activity and cellular response to DNA-damage

PLoS ONE

Volumn 4, Issue 8, 2009, Pages

  Kang, Hyeog ^a   Jung, Jae Won ^a   Kim, Myung K ^a   Chung, Jay H ^a  

^a NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CASEIN KINASE II; PROTEIN P53; SERINE; SIRTUIN 1; SIRT1 PROTEIN, MOUSE;

AGING; AMINO TERMINAL SEQUENCE; ANIMAL CELL; APOPTOSIS; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CARCINOGENESIS; CELL PROTECTION; CONTROLLED STUDY; DEACETYLATION; DNA DAMAGE; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME PHOSPHORYLATION; ENZYME REGULATION; ENZYME SUBSTRATE COMPLEX; HUMAN; HUMAN CELL; IONIZING RADIATION; MOUSE; NONHUMAN; PROTEIN DOMAIN; PROTEIN EXPRESSION; REGULATORY MECHANISM; ACETYLATION; AMINO ACID SEQUENCE; ANIMAL; CELL LINE; CHEMISTRY; DOWN REGULATION; ENZYME SPECIFICITY; IMMUNOPRECIPITATION; METABOLISM; MOLECULAR GENETICS; PHOSPHORYLATION; PHYSIOLOGY; SEQUENCE HOMOLOGY; WESTERN BLOTTING;

EUKARYOTA;

ACETYLATION; AMINO ACID SEQUENCE; ANIMALS; APOPTOSIS; BLOTTING, WESTERN; CASEIN KINASE II; CELL LINE; DNA DAMAGE; DOWN-REGULATION; IMMUNOPRECIPITATION; MICE; MOLECULAR SEQUENCE DATA; PHOSPHORYLATION; SEQUENCE HOMOLOGY, AMINO ACID; SIRTUIN 1; SUBSTRATE SPECIFICITY;

EID: 69949138641     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0006611     Document Type: Article

References (50)

1. Haigis MC, Guarente LP (2006) Mammalian sirtuins-emerging roles in physiology, aging, and calorie restriction. Genes Dev 20: 2913-2921.
2. Imai S, Armstrong CM, Kaeberlein M, Guarente L (2000) Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403: 795-800.
3. Landry J, Sutton A, Tafrov ST, Heller RC, Stebbins J, et al. (2000) The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases. Proc Natl Acad Sci U S A 97: 5807-5811.
4. Gottschling DE, Aparicio OM, Billington BL, Zakian VA (1990) Position effect at S. cerevisiae telomeres: reversible repression of Pol II transcription. Cell 63: 751-762.
5. Rine J, Herskowitz I (1987) Four genes responsible for a position effect on expression from HML and HMR in Saccharomyces cerevisiae. Genetics 116: 9-22.
6. Sinclair DA, Guarente L (1997) Extrachromosomal rDNA circles-a cause of aging in yeast. Cell 91: 1033-1042.
7. Frye RA (1999) Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem Biophys Res Commun 260: 273-279.
8. Cohen HY, Miller C, Bitterman KJ, Wall NR, Hekking B, et al. (2004) Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase. Science 305: 390-392.
9. Rodgers JT, Lerin C, Haas W, Gygi SP, Spiegelman BM, et al. (2005) Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature 434: 113-118.
10. Chen J, Zhou Y, Mueller-Steiner S, Chen LF, Kwon H, et al. (2005) SIRT1 protects against microglia-dependent amyloid-beta toxicity through inhibiting NF-kappaB signaling. J Biol Chem 280: 40364-40374.
11. Kim JE, Chen J, Lou Z (2008) DBC1 is a negative regulator of SIRT1. Nature 451: 583-586.
12. Luo J, Nikolaev AY, Imai S, Chen D, Su F, et al. (2001) Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell 107: 137-148.
13. Yang Y, Fu W, Chen J, Olashaw N, Zhang X, et al. (2007) SIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress. Nat Cell Biol 9: 1253-1262.
14. Zhao W, Kruse JP, Tang Y, Jung SY, Qin J, et al. (2008) Negative regulation of the deacetylase SIRT1 by DBC1. Nature 451: 587-590.
15. Cheng HL, Mostoslavsky R, Saito S, Manis JP, Gu Y, et al. (2003) Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice. Proc Natl Acad Sci U S A 100: 10794-10799.
16. Vaziri H, Dessain SK, Ng Eaton E, Imai SI, Frye RA, et al. (2001) hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase. Cell 107: 149-159.
17. Langley E, Pearson M, Faretta M, Bauer UM, Frye RA, et al. (2002) Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence. Embo J 21: 2383-2396.
18. Litchfield DW (2003) Protein kinase CK2: structure, regulation and role in cellular decisions of life and death. Biochem J 369: 1-15.
19. Pinna LA (2002) Protein kinase CK2: a challenge to canons. J Cell Sci 115: 3873-3878.
20. Faust M, Montenarh M (2000) Subcellular localization of protein kinase CK2. A key to its function? Cell Tissue Res 301: 329-340.
21. Glover CV 3rd (1998) On the physiological role of casein kinase II in Saccharomyces cerevisiae. Prog Nucleic Acid Res Mol Biol 59: 95-133.
22. Duncan JS, Litchfield DW (2008) Too much of a good thing: the role of protein kinase CK2 in tumorigenesis and prospects for therapeutic inhibition of CK2. Biochim Biophys Acta 1784: 33-47.
23. Ahmed K, Gerber DA, Cochet C (2002) Joining the cell survival squad: an emerging role for protein kinase CK2. Trends Cell Biol 12: 226-230.
24. Vilk G, Saulnier RB, St Pierre R, Litchfield DW (1999) Inducible expression of protein kinase CK2 in mammalian cells. Evidence for functional specialization of CK2 isoforms. J Biol Chem 274: 14406-14414.
25. Yamane K, Kinsella TJ (2005) CK2 inhibits apoptosis and changes its cellular localization following ionizing radiation. Cancer Res 65: 4362-4367.
26. Ackerman P, Glover CV, Osheroff N (1990) Stimulation of casein kinase II by epidermal growth factor: relationship between the physiological activity of the kinase and the phosphorylation state of its beta subunit. Proc Natl Acad Sci U S A 87: 821-825.
27. Carroll D, Marshak DR (1989) Serum-stimulated cell growth causes oscillations in casein kinase II activity. J Biol Chem 264: 7345-7348.
28. Kapoor M, Lozano G (1998) Functional activation of p53 via phosphorylation following DNA damage by UV but not gamma radiation. Proc Natl Acad Sci U S A 95: 2834-2837.
29. Keller DM, Zeng X, Wang Y, Zhang QH, Kapoor M, et al. (2001) A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1. Mol Cell 7: 283-292.
30. Pluemsampant S, Safronova OS, Nakahama K, Morita I (2008) Protein kinase CK2 is a key activator of histone deacetylase in hypoxia-associated tumors. Int J Cancer 122: 333-341.
31. Pagano MA, Poletto G, Di Maira G, Cozza G, Ruzzene M, et al. (2007) Tetrabromocinnamic acid (TBCA) and related compounds represent a new class of specific protein kinase CK2 inhibitors. Chembiochem 8: 129-139.
32. Jin Q, Yan T, Ge X, Sun C, Shi X, et al. (2007) Cytoplasm-localized SIRT1 enhances apoptosis. J Cell Physiol 213: 88-97.
33. Tanno M, Sakamoto J, Miura T, Shimamoto K, Horio Y (2007) Nucleocytoplasmic shuttling of the NAD+-dependent histone deacetylase SIRT1. J Biol Chem 282: 6823-6832.
34. McBurney MW, Yang X, Jardine K, Hixon M, Boekelheide K, et al. (2003) The mammalian SIR2alpha protein has a role in embryogenesis and gametogenesis. Mol Cell Biol 23: 38-54.
35. Sakamoto J, Miura T, Shimamoto K, Horio Y (2004) Predominant expression of Sir2alpha, an NAD-dependent histone deacetylase, in the embryonic mouse heart and brain. FEBS Lett 556: 281-286.
36. Gu W, Roeder RG (1997) Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 90: 595-606.
37. Sakaguchi K, Herrera JE, Saito S, Miki T, Bustin M, et al. (1998) DNA damage activates p53 through a phosphorylation-acetylation cascade. Genes Dev 12: 2831-2841.
38. Yeung F, Hoberg JE, Ramsey CS, Keller MD, Jones DR, et al. (2004) Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase. Embo J 23: 2369-2380.
39. Zschoernig B, Mahlknecht U (2009) Carboxy-terminal phosphorylation of SIRT1 by protein kinase CK2. Biochem Biophys Res Commun 381: 372-377.
40. Sasaki T, Maier B, Koclega KD, Chruszcz M, Gluba W, et al. (2008) Phosphorylation regulates SIRT1 function. PLoS ONE 3: e4020.
41. Kim EJ, Kho JH, Kang MR, Um SJ (2007) Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity. Mol Cell 28: 277-290.
42. Meek DW, Simon S, Kikkawa U, Eckhart W (1990) The p53 tumour suppressor protein is phosphorylated at serine 389 by casein kinase II. EMBO J 9: 3253-3260.
43. Hupp TR, Meek DW, Midgley CA, Lane DP (1992) Regulation of the specific DNA binding function of p53. Cell 71: 875-886.
44. Lu H, Taya Y, Ikeda M, Levine AJ (1998) Ultraviolet radiation, but not gamma radiation or etoposide-induced DNA damage, results in the phosphorylation of the murine p53 protein at serine-389. Proc Natl Acad Sci U S A 95: 6399-6402.
45. Chen WY, Wang DH, Yen RC, Luo J, Gu W, et al. (2005) Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses. Cell 123: 437-448.
46. Huffman DM, Grizzle WE, Bamman MM, Kim JS, Eltoum IA, et al. (2007) SIRT1 is significantly elevated in mouse and human prostate cancer. Cancer Res 67: 6612-6618.
47. Ryu SW, Woo JH, Kim YH, Lee YS, Park JW, et al. (2006) Downregulation of protein kinase CKII is associated with cellular senescence. FEBS Lett 580: 988-994.
48. Sasaki T, Maier B, Bartke A, Scrable H (2006) Progressive loss of SIRT1 with cell cycle withdrawal. Aging Cell 5: 413-422.
49. Wang RH, Sengupta K, Li C, Kim HS, Cao L, et al. (2008) Impaired DNA damage response, genome instability, and tumorigenesis in SIRT1 mutant mice. Cancer Cell 14: 312-323.
50. Firestein R, Blander G, Michan S, Oberdoerffer P, Ogino S, et al. (2008) The SIRT1 deacetylase suppresses intestinal tumorigenesis and colon cancer growth. PLoS ONE 3: e2020.