A prevalent cancer susceptibility APOBEC3A hybrid allele bearing APOBEC3B 3′UTR enhances chromosomal DNA damage

Nature Communications

Volumn 5, Issue , 2014, Pages

  Caval, Vincent ^a   Suspène, Rodolphe ^a   Shapira, Milana ^a   Vartanian, Jean Pierre ^a   Wain Hobson, Simon ^a  

^a INSTITUT PASTEUR   (France)

Author keywords

[No Author keywords available]

Indexed keywords

3' AZIDO 2',3' DIDEOXY 5 METHYLCYTIDINE; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3A; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3B; CELL NUCLEUS DNA; CYTIDINE DEAMINASE; MESSENGER RNA; UNCLASSIFIED DRUG; 3' UNTRANSLATED REGION; APOBEC3A PROTEIN, HUMAN; APOBEC3B PROTEIN, HUMAN; PROTEIN;

ALLELE; CANCER; CATALYSIS; CHROMOSOME; DISEASE INCIDENCE; GENE EXPRESSION; GENOTOXICITY; HEALTH RISK; MUTATION; RNA;

3' UNTRANSLATED REGION; ALLELE; ARTICLE; CANCER SUSCEPTIBILITY; CHROMOSOME DAMAGE; DEAMINATION; DNA DAMAGE; ESCHERICHIA COLI; FEMALE; HUMAN; HUMAN CELL; NONHUMAN; SOMATIC MUTATION; GENETIC PREDISPOSITION; GENETICS; HEK293 CELL LINE; HELA CELL LINE; MUTATION; NEOPLASM; TUMOR CELL LINE;

FAR EAST;

3' UNTRANSLATED REGIONS; ALLELES; CELL LINE, TUMOR; CYTIDINE DEAMINASE; DNA DAMAGE; GENETIC PREDISPOSITION TO DISEASE; HEK293 CELLS; HELA CELLS; HUMANS; MUTATION; NEOPLASMS; PROTEINS;

EID: 84923309215     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms6129     Document Type: Article

References (41)

1. Jarmuz, A. et al. An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22. Genomics 79, 285-296 (2002).
2. Landry, S., Narvaiza, I., Linfesty, D. C. & Weitzman, M. D. APOBEC3A can activate the DNA damage response and cause cell-cycle arrest. EMBO Rep. 12, 444-450 (2011).
3. Mussil, B. et al. Human APOBEC3A isoforms translocate to the nucleus and induce DNA double strand breaks leading to cell stress and death. PLoS ONE 8, e73641 (2013).
4. Suspène, R. et al. Somatic hypermutation of human mitochondrial and nuclear DNA by APOBEC3 cytidine deaminases, a pathway for DNA catabolism. Proc. Natl Acad. Sci. USA 108, 4858-4863 (2011).
5. Carpenter, M. A. et al. Methylcytosine and normal cytosine deamination by the foreign DNA restriction enzyme APOBEC3A. J. Biol. Chem. 287, 34801-34808 (2012).
6. Suspène, R., Aynaud, M. M., Vartanian, J. P. & Wain-Hobson, S. Efficient deamination of 5-methylcytidine and 5-substituted cytidine residues in DNA by human APOBEC3A cytidine deaminase. PLoS ONE 8, e63461 (2013).
7. Wijesinghe, P. & Bhagwat, A. S. Efficient deamination of 5-methylcytosines in DNA by human APOBEC3A, but not by AID or APOBEC3G. Nucleic Acids Res. 40, 9206-9217 (2012).
8. Greenman, C. et al. Patterns of somatic mutation in human cancer genomes. Nature 446, 153-158 (2007).
9. Nik-Zainal, S. et al. Mutational processes molding the genomes of 21 breast cancers. Cell 149, 979-993 (2012).
10. Stephens, P. J. et al. Complex landscapes of somatic rearrangement in human breast cancer genomes. Nature 462, 1005-1010 (2009).
11. Stephens, P. J. et al. The landscape of cancer genes and mutational processes in breast cancer. Nature 486, 400-404 (2012).
12. Alexandrov, L. B. et al. Signatures of mutational processes in human cancer. Nature 500, 415-421 (2013).
13. Roberts, S. A. et al. An APOBEC cytidine deaminase mutagenesis pattern is widespread in human cancers. Nat. Genet. 45, 970-976 (2013).
14. Roberts, S. A. & Gordenin, D. A. Clustered and genome-wide transient mutagenesis in human cancers: Hypermutation without permanent mutators or loss of fitness. Bioessays 36, 382-393 (2014).
15. Doehle, B. P., Schafer, A., Wiegand, H. L., Bogerd, H. P. & Cullen, B. R. Differential sensitivity of murine leukemia virus to APOBEC3-mediated inhibition is governed by virion exclusion. J. Virol. 79, 8201-8207 (2005).
16. Mahieux, R. et al. Extensive editing of a small fraction of human T-cell leukemia virus type 1 genomes by four APOBEC3 cytidine deaminases. J. Gen. Virol. 86, 2489-2494 (2005).
17. Ooms, M., Krikoni, A., Kress, A. K., Simon, V. & Munk, C. APOBEC3A, APOBEC3B, and APOBEC3H haplotype 2 restrict human T-lymphotropic virus type 1. J. Virol. 86, 6097-6108 (2012).
18. Bonvin, M. & Greeve, J. Effects of point mutations in the cytidine deaminase domains of APOBEC3B on replication and hypermutation of hepatitis B virus in vitro. J. Gen. Virol. 88, 3270-3274 (2007).
19. Suspène, R. et al. Extensive editing of both hepatitis B virus DNA strands by APOBEC3 cytidine deaminases in vitro and in vivo. Proc. Natl Acad. Sci. USA 102, 8321-8326 (2005).
20. Burns, M. B. et al. APOBEC3B is an enzymatic source of mutation in breast cancer. Nature 494, 366-370 (2013).
21. Shinohara, M. et al. APOBEC3B can impair genomic stability by inducing base substitutions in genomic DNA in human cells. Sci. Rep. 2, 806 (2012).
22. Suspène, R. et al. Erroneous identification of APOBEC3-edited chromosomal DNA in cancer genomics. Br. J. Cancer. 110, 2615-2622 (2014).
23. Komatsu, A., Nagasaki, K., Fujimori, M., Amano, J. & Miki, Y. Identification of novel deletion polymorphisms in breast cancer. Int J. Oncol. 33, 261-270 (2008).
24. Long, J. et al. A common deletion in the APOBEC3 genes and breast cancer risk. J. Natl Cancer Inst. 105, 573-579 (2013).
25. Xuan, D. et al. APOBEC3 deletion polymorphism is associated with breast cancer risk among women of European ancestry. Carcinogenesis 34, 2240-2243 (2013).
26. Zhang, T. et al. Evidence of associations of APOBEC3B gene deletion with susceptibility to persistent HBV infection and hepatocellular carcinoma. Hum. Mol. Genet. 22, 1262-1269 (2012).
27. Nik-Zainal, S. et al. Association of a germline copy number polymorphism of APOBEC3A and APOBEC3B with burden of putative APOBEC-dependent mutations in breast cancer. Nat. Genet. 46, 487-491 (2014).
28. Kidd, J. M., Newman, T. L., Tuzun, E., Kaul, R. & Eichler, E. E. Population stratification of a common APOBEC gene deletion polymorphism. PLoS Genet. 3, e63 (2007).
29. Yu, Q. et al. APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication. J. Biol. Chem. 279, 53379-53386 (2004).
30. Kinomoto, M. et al. All APOBEC3 family proteins differentially inhibit LINE-1 retrotransposition. Nucleic Acids Res. 35, 2955-2964 (2007).
31. Caval, V., Suspène, R., Vartanian, J. P. & Wain-Hobson, S. Orthologous mammalian APOBEC3A cytidine deaminases hypermutate nuclear DNA. Mol. Biol. Evol. 31, 330-340 (2014).
32. McDougle, R. M., Hultquist, J. F., Stabell, A. C., Sawyer, S. L. & Harris, R. S. D316 is critical for the enzymatic activity and HIV-1 restriction potential of human and rhesus APOBEC3B. Virology 441, 31-39 (2013).
33. Stenglein, M. D., Burns, M. B., Li, M., Lengyel, J. & Harris, R. S. APOBEC3 proteins mediate the clearance of foreign DNA from human cells. Nat. Struct. Mol. Biol. 17, 222-229 (2010).
34. Henry, M. et al. Genetic editing of HBV DNA by monodomain human APOBEC3 cytidine deaminases and the recombinant nature of APOBEC3G. PLoS ONE 4, e4277 (2009).
35. Suspène, R., Henry, M., Guillot, S., Wain-Hobson, S. & Vartanian, J. P. Recovery of APOBEC3-edited human immunodeficiency virus G-4A hypermutants by differential DNA denaturation PCR. J. Gen. Virol. 86, 125-129 (2005).
36. Pham, P., Landolph, A., Mendez, C., Li, N. & Goodman, M. F. A biochemical analysis linking APOBEC3A to disparate HIV-1 restriction and skin cancer. J. Biol. Chem. 288, 29294-29304 (2013).
37. Jones, P. A. & Baylin, S. B. The epigenomics of cancer. Cell 128, 683-692 (2007).
38. Madsen, P. et al. Psoriasis upregulated phorbolin-1 shares structural but not functional similarity to the mRNA-editing protein apobec-1. J. Invest. Dermatol. 113, 162-169 (1999).
39. Koning, F. A. et al. Defining APOBEC3 expression patterns in human tissues and hematopoietic cell subsets. J. Virol. 83, 9474-9485 (2009).
40. Refsland, E. W. et al. Quantitative profiling of the full APOBEC3 mRNA repertoire in lymphocytes and tissues: implications for HIV-1 restriction. Nucleic Acids Res. 38, 4274-4284 (2010).
41. Balkwill, F. & Mantovani, A. Inflammation and cancer: back to Virchow? Lancet 357, 539-545 (2001).