Toward specific functions of poly(ADP-ribose) polymerase-2

Trends in Molecular Medicine

Volumn 14, Issue 4, 2008, Pages 169-178

  Yélamos, José ^a   Schreiber, Valérie ^b   Dantzer, Françoise ^b  

^a HOSPITAL DEL MAR   (Spain)

^b UNIVERSITÉ DE STRASBOURG   (France)

Author keywords

[No Author keywords available]

Indexed keywords

NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 2;

ADIPOGENESIS; CATALYSIS; CELL DEATH; CELL DIFFERENTIATION; CELL MATURATION; CENTROMERE; CRYSTAL STRUCTURE; DNA STRAND BREAKAGE; ENZYME ACTIVITY; ENZYME SPECIFICITY; EXCISION REPAIR; GENOME; GERM CELL; HETEROCHROMATIN; MALE FERTILITY; NONHUMAN; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; REVIEW; SINGLE STRANDED DNA BREAK; SPERMATOGENESIS; T LYMPHOCYTE;

ANIMALS; CELL DIFFERENTIATION; DNA DAMAGE; GENOME; HUMANS; INFLAMMATION; POLY(ADP-RIBOSE) POLYMERASES;

EID: 41549155890     PISSN: 14714914     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molmed.2008.02.003     Document Type: Review

References (77)

1. Schreiber V., et al. Poly(ADP-ribose): novel functions for an old molecule. Nat. Rev. Mol. Cell Biol. 7 (2006) 517-528
2. Jagtap P., and Szabo C. Poly(ADP-ribose) polymerase and the therapeutic effects of its inhibitors. Nat. Rev. Drug Discov. 4 (2005) 421-440
3. Ame J.C., et al. The PARP superfamily. Bioessays 26 (2004) 882-893
4. Otto H., et al. In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs). BMC Genomics 6 (2005) 139
5. Ame J.C., et al. PARP-2, a novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase. J. Biol. Chem. 274 (1999) 17860-17868
6. Schreiber V., et al. Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1. J. Biol. Chem. 277 (2002) 23028-23036
7. Dantzer F., et al. Base excision repair is impaired in mammalian cells lacking Poly(ADP-ribose) polymerase-1. Biochemistry 39 (2000) 7559-7569
8. Ménissier D.M.J., et al. Functional interaction between PARP-1 and PARP-2 in chromosome stability and embryonic development in mouse. EMBO J. 22 (2003) 2255-2263
9. Johansson M. A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues. Genomics 57 (1999) 442-445
10. Berghammer H., et al. pADPRT-2: a novel mammalian polymerizing(ADP-ribosyl)transferase gene related to truncated pADPRT homologues in plants and Caenorhabditis elegans. FEBS Lett. 449 (1999) 259-263
11. Pion E., et al. DNA-induced dimerization of poly(ADP-ribose) polymerase-1 triggers its activation. Biochemistry 44 (2005) 14670-14681
12. Schreiber V., et al. PARP-2, structure-function relationship. In: Burkle A. (Ed). Poly(ADP-ribosyl)ation (2004), Landes Bioscience 13-31
13. Langelier M.F., et al. A third zinc-binding domain of human PARP-1 coordinates DNA-dependent enzyme activation. J. Biol. Chem. 283 (2008) 4105-4114
14. Ruf A., et al. Structure of the catalytic fragment of poly(AD-ribose) polymerase from chicken. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 7481-7485
15. Oliver A.W., et al. Crystal structure of the catalytic fragment of murine poly(ADP-ribose) polymerase-2. Nucleic Acids Res. 32 (2004) 456-464
16. Lengauer C., et al. Genetic instabilities in human cancers. Nature 396 (1998) 643-649
17. Trucco C., et al. DNA repair defect in poly(ADP-ribose) polymerase-deficient cell lines. Nucleic Acids Res. 26 (1998) 2644-2649
18. Fisher A.E., et al. Poly(ADP-ribose) polymerase 1 accelerates single-strand break repair in concert with poly(ADP-ribose) glycohydrolase. Mol. Cell. Biol. 27 (2007) 5597-5605
19. Mortusewicz O., et al. Feedback-regulated poly(ADP-ribosyl)ation by PARP-1 is required for rapid response to DNA damage in living cells. Nucleic Acids Res. 35 (2007) 7665-7675
20. Okano S., et al. Spatial and temporal cellular responses to single-strand breaks in human cells. Mol. Cell. Biol. 23 (2003) 3974-3981
21. Lan L., et al. In situ analysis of repair processes for oxidative DNA damage in mammalian cells. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 13738-13743
22. El Khamisy S.F., et al. A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage. Nucleic Acids Res. 31 (2003) 5526-5533
23. Menisser-de Murcia J., et al. Early embryonic lethality in PARP-1 Atm double-mutant mice suggests a functional synergy in cell proliferation during development. Mol. Cell. Biol. 21 (2001) 1828-1832
24. Huber A., et al. PARP-1, PARP-2 and ATM in the DNA damage response: functional synergy in mouse development. DNA Repair (Amst.) 3 (2004) 1103-1108
25. Haince J.F., et al. Ataxia telangiectasia mutated (ATM) signaling network is modulated by a novel poly(ADP-ribose)-dependent pathway in the early response to DNA-damaging agents. J. Biol. Chem. 282 (2007) 16441-16453
26. Aguilar-Quesada R., et al. Interaction between ATM and PARP-1 in response to DNA damage and sensitization of ATM deficient cells through PARP inhibition. BMC Mol. Biol. 8 (2007) 29
27. Haince J.F., et al. PARP1-dependent kinetics of recruitment of MRE11 and NBS1 proteins to multiple DNA damage sites. J. Biol. Chem. 283 (2008) 1197-1208
28. Wang M., et al. PARP-1 and Ku compete for repair of DNA double strand breaks by distinct NHEJ pathways. Nucleic Acids Res. 34 (2006) 6170-6182
29. Audebert M., et al. Involvement of poly(ADP-ribose) polymerase-1 and XRCC1/DNA ligase III in an alternative route for DNA double-strand breaks rejoining. J. Biol. Chem. 279 (2004) 55117-55126
30. Rosidi B., et al. Histone H1 functions as a stimulatory factor in backup pathways of NHEJ. Nucleic Acids Res. (2008). http://nar.oxfordjournals.org 10.1093/nar/gkn013
31. Li B., et al. Identification and biochemical characterization of a Werner's syndrome protein complex with Ku70/80 and poly(ADP-ribose) polymerase-1. J. Biol. Chem. 279 (2004) 13659-13667
32. Galande S., and Kohwi-Shigematsu T. Poly(ADP-ribose) polymerase and Ku autoantigen form a complex and synergistically bind to matrix attachment sequences. J. Biol. Chem. 274 (1999) 20521-20528
33. Chalmers A., et al. PARP-1, PARP-2, and the cellular response to low doses of ionizing radiation. Int. J. Radiat. Oncol. Biol. Phys. 58 (2004) 410-419
34. Marples B. Is low-dose hyper-radiosensitivity a measure of G2-phase cell radiosensitivity?. Cancer Metastasis Rev. 23 (2004) 197-207
35. Saxena A., et al. Poly(ADP-ribose) polymerase 2 localizes to mammalian active centromeres and interacts with PARP-1, Cenpa, Cenpb and Bub3, but not Cenpc. Hum. Mol. Genet. 11 (2002) 2319-2329
36. Saxena A., et al. Centromere proteins Cenpa, Cenpb, and Bub3 interact with poly(ADP-ribose) polymerase-1 protein and are poly(ADP-ribosyl)ated. J. Biol. Chem. 277 (2002) 26921-26926
37. Earle E., et al. Poly(ADP-ribose) polymerase at active centromeres and neocentromeres at metaphase. Hum. Mol. Genet. 9 (2000) 187-194
38. Dantzer F., et al. Poly(ADP-ribose) polymerase-2 contributes to the fidelity of male meiosis I and spermiogenesis. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 14854-14859
39. Blasco M.A. The epigenetic regulation of mammalian telomeres. Nat. Rev. Genet. 8 (2007) 299-309
40. Dantzer F., et al. Functional interaction between poly(ADP-Ribose) polymerase 2 (PARP-2) and TRF2: PARP activity negatively regulates TRF2. Mol. Cell. Biol. 24 (2004) 1595-1607
41. Muftuoglu M., et al. Telomere repeat binding factor 2 interacts with base excision repair proteins and stimulates DNA synthesis by DNA polymerase beta. Cancer Res. 66 (2006) 113-124
42. Wright W.E., and Shay J.W. Telomere-binding factors and general DNA repair. Nat. Genet. 37 (2005) 116-118
43. Griffith J.D., et al. Mammalian telomeres end in a large duplex loop. Cell 97 (1999) 503-514
44. Cook B.D., et al. Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres. Mol. Cell. Biol. 22 (2002) 332-342
45. Gomez M., et al. PARP1 Is a TRF2-associated poly(ADP-ribose)polymerase and protects eroded telomeres. Mol. Biol. Cell 17 (2006) 1686-1696
46. Brown C.J., and Greally J.M. A stain upon the silence: genes escaping X inactivation. Trends Genet. 19 (2003) 432-438
47. Nusinow D.A., et al. Poly(ADP-ribose) polymerase 1 is inhibited by a histone H2A variant, MacroH2A, and contributes to silencing of the inactive X chromosome. J. Biol. Chem. 282 (2007) 12851-12859
48. de Murcia J.M., et al. Requirement of poly(ADP-ribose) polymerase in recovery from DNA damage in mice and in cells. P.N.A.S. 94 (1997) 7303-7307
49. Bryan T.M., et al. Evidence for an alternative mechanism for maintaining telomere length in human tumors and tumor-derived cell lines. Nat. Med. 3 (1997) 1271-1274
50. Meder V.S., et al. PARP-1 and PARP-2 interact with nucleophosmin/B23 and accumulate in transcriptionally active nucleoli. J. Cell Sci. 118 (2005) 211-222
51. Borggrefe T., et al. A B-cell-specific DNA recombination complex. J. Biol. Chem. 273 (1998) 17025-17035
52. Ramsamooj P., et al. Modification of nucleolar protein B23 after exposure to ionizing radiation. Radiat. Res. 143 (1995) 158-164
53. Tramontano F., et al. Differential contribution of poly(ADPR)polymerase-1 and 2 (PARP-1 and 2) to the poly(ADP-ribosyl)ation reaction in rat primary spermatocytes. Mol. Hum. Reprod. 13 (2007) 821-828
54. Bai P., et al. Peroxisome proliferator-activated receptor (PPAR)-2 controls adipocyte differentiation and adipose tissue function through the regulation of the activity of the retinoid X receptor/PPARγ heterodimer. J. Biol. Chem. 282 (2007) 37738-37746
55. Maeda Y., et al. PARP-2 interacts with TTF-1 and regulates expression of surfactant protein-B. J. Biol. Chem. 281 (2006) 9600-9606
56. Yelamos J., et al. PARP-2 deficiency affects the survival of CD4+CD8+ double-positive thymocytes. EMBO J. 25 (2006) 4350-4360
57. Strasser A. The role of BH3-only proteins in the immune system. Nat. Rev. Immunol. 5 (2005) 189-200
58. Xi H., and Kersh G.J. Sustained early growth response gene 3 expression inhibits the survival of CD4/CD8 double-positive thymocytes. J. Immunol. 173 (2004) 340-348
59. Mota R.A., et al. Inhibition of poly(ADP-ribose) polymerase attenuates the severity of acute pancreatitis and associated lung injury. Lab. Invest. 85 (2005) 1250-1262
60. Jijon H.B., et al. Inhibition of poly(ADP-ribose) polymerase attenuates inflammation in a model of chronic colitis. Am. J. Physiol. Gastrointest. Liver Physiol. 279 (2000) G641-G651
61. Oliver F.J., et al. Resistance to endotoxic shock as a consequence of defective NF-kappaB activation in poly (ADP-ribose) polymerase-1 deficient mice. EMBO J. 18 (1999) 4446-4454
62. Hassa P.O., et al. Acetylation of poly(ADP-ribose) polymerase-1 by p300/CREB-binding protein regulates coactivation of NF-kappaB-dependent transcription. J. Biol. Chem. 280 (2005) 40450-40464
63. Carrillo A., et al. Transcription regulation of TNF-alpha-early response genes by poly(ADP-ribose) polymerase-1 in murine heart endothelial cells. Nucleic Acids Res. 32 (2004) 757-766
64. Moubarak R.S., et al. Sequential activation of poly(ADP-ribose) polymerase 1, calpains, and Bax is essential in apoptosis-inducing factor-mediated programmed necrosis. Mol. Cell. Biol. 27 (2007) 4844-4862
65. Popoff I., et al. Antisense oligonucleotides to poly(ADP-ribose) polymerase-2 ameliorate colitis in interleukin-10-deficient mice. J. Pharmacol. Exp. Ther. 303 (2002) 1145-1154
66. Kofler J., et al. Differential effect of PARP-2 deletion on brain injury after focal and global cerebral ischemia. J. Cereb. Blood Flow Metab. 26 (2006) 135-141
67. Durkacz B.W., et al. (ADP-ribose)n participates in DNA excision repair. Nature 283 (1980) 593-596
68. Ratnam K., and Low J.A. Current development of clinical inhibitors of poly(ADP-ribose) polymerase in oncology. Clin. Cancer Res. 13 (2007) 1383-1388
69. Pacher P., and Szabo C. Role of poly(ADP-ribose) polymerase 1 (PARP-1) in cardiovascular diseases: the therapeutic potential of PARP inhibitors. Cardiovasc. Drug Rev. 25 (2007) 235-260
70. Farmer H., et al. Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy. Nature 434 (2005) 917-921
71. Perkins E., et al. Novel inhibitors of poly(ADP-ribose) polymerase/PARP1 and PARP2 identified using a cell-based screen in yeast. Cancer Res. 61 (2001) 4175-4183
72. Miwa M., and Masutani M. PolyADP-ribosylation and cancer. Cancer Sci. 98 (2007) 1528-1535
73. Poirier G.G., et al. Poly(ADP-ribosyl)ation of polynucleosomes causes relaxation of chromatin structure. Proc. Natl. Acad. Sci. U. S. A. 79 (1982) 3423-3427
74. Pleschke J.M., et al. Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins. J. Biol. Chem. 275 (2000) 40974-40980
75. Ahel I., et al. Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins. Nature 451 (2008) 81-85
76. Karras G.I., et al. The macro domain is an ADP-ribose binding module. EMBO J. 24 (2005) 1911-1920
77. von Kobbe C., et al. Poly(ADP-ribose) polymerase 1 regulates both the exonuclease and helicase activities of the Werner syndrome protein. Nucleic Acids Res. 32 (2004) 4003-4014