Regulation of Aicda expression and AID activity

References

• Xu Z., Zan H., Pone E. J., Mai T., Casali P.. Immunoglobulin class switching: induction, targeting and beyond. Nature Rev. Immunol.. 2012; 12:517–531.
   PubMed Web of Science ®Google Scholar
• Zan H., White C. A., Thomas L. M., . Rev1 recruits Ung to switch regions and enhances dU deglycosylation for immunoglobulin class switch DNA recombination. Cell Repts.. 2012; 2:1220–1232.
   PubMed Web of Science ®Google Scholar
• Marusawa H., Chiba T.. Helicobacter pylori-induced activation-induced cytidine deaminase expression and carcinogenesis. Curr. Opin. Immunol.. 2010; 22:442–447.
   PubMed Web of Science ®Google Scholar
• Marusawa H., Takai A., Chiba T.. Role of activation-induced cytidine deaminase in inflammation-associated cancer development. Adv. Immunol.. 2011; 111:109–141.
   Google Scholar
• Xu Z., Pone E. J., Al-Qahtani A., . Regulation of aicda expression and AID activity: relevance to somatic hypermutation and class switch DNA recombination. Crit. Rev. Immunol.. 2007; 27:367–397.
   PubMed Web of Science ®Google Scholar
• Stavnezer J.. Complex regulation and function of activation-induced cytidine deaminase. Trends Immunol.. 2011; 32:194–201.
   PubMedGoogle Scholar
• Kuraoka M., Holl T. M., Liao D., . Activation-induced cytidine deaminase mediates central tolerance in B cells. Proc. Natl. Acad. Sci. USA. 2011; 108:11560–11565.
   PubMed Web of Science ®Google Scholar
• Meyers G., Ng Y. S., Bannock J. M., . Activation-induced cytidine deaminase (AID) is required for B-cell tolerance in humans. Proc. Natl. Acad. Sci. USA. 2011; 108:11554–11559.
   PubMed Web of Science ®Google Scholar
• Pasqualucci L., Bhagat G., Jankovic M., . AID is required for germinal center-derived lymphomagenesis. Nat. Genet.. 2008; 40:108–112.
   PubMed Web of Science ®Google Scholar
• Robbiani D. F., Bunting S., Feldhahn N., . AID produces DNA double-strand breaks in non-Ig genes and mature B cell lymphomas with reciprocal chromosome translocations. Mol. Cell. 2009; 36:631–641.
   PubMed Web of Science ®Google Scholar
• Hasham M. G., Donghia N. M., Coffey E., . Widespread genomic breaks generated by activation-induced cytidine deaminase are prevented by homologous recombination. Nat. Immunol.. 2010; 11:820–826.
   Google Scholar
• Ramiro A. R., Jankovic M., Eisenreich T., . AID is required for c-Myc/IgH chromosome translocations in vivo. Cell. 2004; 118:431–438.
   PubMed Web of Science ®Google Scholar
• Robbiani D. F., Bothmer A., Callen E., . AID is required for the chromosomal breaks in c-myc that lead to c-myc/IgH translocations. Cell. 2008; 135:1028–1038.
   PubMed Web of Science ®Google Scholar
• Delker R. K., Fugmann S. D., Papavasiliou F. N.. A coming-of-age story: activation-induced cytidine deaminase turns 10. Nat. Immunol.. 2009; 10:1147–1153.
   Google Scholar
• Hasler J., Rada C., Neuberger M. S.. Cytoplasmic activation-induced cytidine deaminase (AID) exists in stoichiometric complex with translation elongation factor 1α (eEF1A). Proc. Natl. Acad. Sci. USA. 2011; 108:18366–18371.
   PubMedGoogle Scholar
• Aoufouchi S., Faili A., Zober C., . Proteasomal degradation restricts the nuclear lifespan of AID. J. Exp. Med.. 2008; 205:1357–1368.
   PubMed Web of Science ®Google Scholar
• Uchimura Y., Barton L. F., Rada C., Neuberger M. S.. REG-γ associates with and modulates the abundance of nuclear activation-induced deaminase. J. Exp. Med.. 2011; 208:2385–2891.
   Google Scholar
• Li G., Pone E. J., Mai T., . Iron inhibits activation-induced cytidine deaminase enzymatic activity and modulates immunoglobulin class switch DNA recombination. J. Biol. Chem.. 2012; 287:21520–21529.
   PubMedGoogle Scholar
• Shinkura R., Ito S., Begum N. A., . Separate domains of AID are required for somatic hypermutation and class-switch recombination. Nat. Immunol.. 2004; 5:707–712.
   PubMed Web of Science ®Google Scholar
• Pone E. J., Zhang J., Mai T., . BCR-signalling synergizes with TLR-signalling for induction of AID and immunoglobulin class-switching through the non-canonical NF-κB pathway. Nat. Commun.. 2012; 3:767.
   PubMed Web of Science ®Google Scholar
• Bishop G. A., Hostager B. S.. The CD40-CD154 interaction in B cell-T cell liaisons. Cytokine Growth Factor Rev.. 2003; 14:297–309.
   PubMedGoogle Scholar
• Graham J. P., Arcipowski K. M., Bishop G. A.. Differential B-lymphocyte regulation by CD40 and its viral mimic, latent membrane protein 1. Immunol. Rev.. 2010; 237:226–248.
   PubMedGoogle Scholar
• Rickert R. C., Jellusova J., Miletic A. V.. Signaling by the tumor necrosis factor receptor superfamily in B-cell biology and disease. Immunol. Rev.. 2011; 244:115–133.
   PubMed Web of Science ®Google Scholar
• Oeckinghaus A., Hayden M. S., Ghosh S.. Crosstalk in NF-κB signaling pathways. Nat. Immunol.. 2011; 12:695–708.
   PubMed Web of Science ®Google Scholar
• Sun S. C.. Non-canonical NF-κB signaling pathway. Cell Res.. 2011; 21:71–85.
   PubMed Web of Science ®Google Scholar
• Tran T. H., Nakata M., Suzuki K., . B cell-specific and stimulation-responsive enhancers derepress Aicda by overcoming the effects of silencers. Nat. Immunol.. 2010; 11:148–154.
   PubMedGoogle Scholar
• Cerutti A.. The regulation of IgA class switching. Nat. Rev. Immunol.. 2008; 8:421–434.
   PubMed Web of Science ®Google Scholar
• Fagarasan S., Kawamoto S., Kanagawa O., Suzuki K.. Adaptive immune regulation in the gut: T cell-dependent and T cell-independent IgA synthesis. Annu. Rev. Immunol.. 2010; 28:243–273.
   PubMed Web of Science ®Google Scholar
• Cerutti A., Chen K., Chorny A.. Immunoglobulin responses at the mucosal interfaces. Annu. Rev. Immunol.. 2011; 29:273–293.
   PubMed Web of Science ®Google Scholar
• Bossen C., Schneider P.. BAFF, APRIL and their receptors: structure, function and signaling. Semin. Immunol.. 2006; 18:263–275.
   PubMed Web of Science ®Google Scholar
• Mackay F., Schneider P.. Cracking the BAFF code. Nat. Rev. Immunol.. 2009; 9:491–502.
   PubMed Web of Science ®Google Scholar
• He B., Qiao X., Cerutti A.. CpG DNA induces IgG class switch DNA recombination by activating human B cells through an innate pathway that requires TLR9 and cooperates with IL-10. J. Immunol.. 2004; 173:4479–4491.
   PubMed Web of Science ®Google Scholar
• Xu W., Santini P. A., Matthews A. J., . Viral double-stranded RNA triggers Ig class switching by activating upper respiratory mucosa B cells through an innate TLR3 pathway involving BAFF. J. Immunol.. 2008; 181:276–287.
   PubMed Web of Science ®Google Scholar
• He B., Santamaria R., Xu W., . The transmembrane activator TACI triggers immunoglobulin class switching by activating B cells through the adaptor MyD88. Nat. Immunol.. 2010; 11:836–845.
   PubMed Web of Science ®Google Scholar
• Bombardieri M., Kam N. W., Brentano F., . A BAFF/APRIL-dependent TLR3-stimulated pathway enhances the capacity of rheumatoid synovial fibroblasts to induce AID expression and Ig class-switching in B cells. Ann. Rheum. Dis.. 2011; 70:1857–1865.
   PubMedGoogle Scholar
• Vos Q., Lees A., Wu Z. Q., Snapper C. M., Mond J. J.. B-cell activation by T-cell-independent type 2 antigens as an integral part of the humoral immune response to pathogenic microorganisms. Immunol. Rev.. 2000; 176:154–170.
   PubMed Web of Science ®Google Scholar
• Coutinho A., Poltorack A.. Innate immunity: from lymphocyte mitogens to Toll-like receptors and back. Curr. Opin. Immunol.. 2003; 15:599–602.
   PubMedGoogle Scholar
• Pone E. J., Zan H., Zhang J., . Toll-like receptors and B-cell receptors synergize to induce immunoglobulin class-switch DNA recombination: relevance to microbial antibody responses. Crit. Rev. Immunol.. 2010; 30:1–29.
   PubMedGoogle Scholar
• Pone E. J., Xu Z., White C. A., Zan H., Casali P.. B cell TLRs and induction of immunoglobulin class-switch DNA recombination. Front. Biosci.. 2012; 17:2594–2615.
   PubMedGoogle Scholar
• Medzhitov R.. Recognition of microorganisms and activation of the immune response. Nature. 2007; 449:819–826.
   PubMed Web of Science ®Google Scholar
• Lee M. S., Kim Y. J.. Signaling pathways downstream of pattern-recognition receptors and their cross talk. Annu. Rev. Biochem.. 2007; 76:447–480.
   PubMed Web of Science ®Google Scholar
• Kawai T., Akira S.. The roles of TLRs, RLRs and NLRs in pathogen recognition. Int. Immunol.. 2009; 21:317–337.
   PubMed Web of Science ®Google Scholar
• Gururajan M., Jacob J., Pulendran B.. Toll-like receptor expression and responsiveness of distinct murine splenic and mucosal B-cell subsets. PLoS One. 2007; 2:e863.
   Google Scholar
• Coutinho A., Moller G.. Thymus-independent B-cell induction and paralysis. Adv. Immunol.. 1975; 21:113–236.
   PubMedGoogle Scholar
• Pike B. L., Alderson M. R., Nossal G. J.. T-independent activation of single B cells: an orderly analysis of overlapping stages in the activation pathway. Immunol. Rev.. 1987; 99:119–152.
   PubMedGoogle Scholar
• Medzhitov R., Preston-Hurlburt P., Janeway C. A.Jr. A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature. 1997; 388:394–397.
   PubMed Web of Science ®Google Scholar
• Poltorak A., He X., Smirnova I., . Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: mutations in Tlr4 gene. Science. 1998; 282:2085–2088.
   PubMed Web of Science ®Google Scholar
• Poxton I. R.. Antibodies to lipopolysaccharide. J. Immunol. Meth.. 1995; 186:1–15.
   PubMedGoogle Scholar
• Quintana F. J., Solomon A., Cohen I. R., Nussbaum G.. Induction of IgG3 to LPS via Toll-like receptor 4 co-stimulation. PLoS One. 2008; 3:e3509.
   Google Scholar
• Chaturvedi A., Dorward D., Pierce S. K.. The B cell receptor governs the subcellular location of Toll-like receptor 9 leading to hyperresponses to DNA-containing antigens. Immunity. 2008; 28:799–809.
   PubMed Web of Science ®Google Scholar
• Chaturvedi A., Pierce S. K.. How location governs Toll-like receptor signaling. Traffic. 2009; 10:621–628.
   PubMed Web of Science ®Google Scholar
• Gu X., Shivarov V., Strout M. P.. The role of activation-induced cytidine deaminase in lymphomagenesis. Curr. Opin. Hematol.. 2012; 19:292–298.
   PubMed Web of Science ®Google Scholar
• Sernández I. V., de Yébenes V. G., Dorsett Y., Ramiro A. R.. Haploinsufficiency of activation-induced deaminase for antibody diversification and chromosome translocations both in vitro and in vivo. PLoS One. 2008; 3:e3927.
   PubMed Web of Science ®Google Scholar
• Takizawa M., Tolarova H., Li Z., . AID expression levels determine the extent of cMyc oncogenic translocations and the incidence of B cell tumor development. J. Exp. Med.. 2008; 205:1949–1957.
   PubMed Web of Science ®Google Scholar
• Zan H., Zhang J., Ardeshna S., . Lupus-prone MRL/Faslpr/lpr mice display increased AID expression and extensive DNA lesions, comprising deletions and insertions, in the immunoglobulin locus: concurrent up-regulation of somatic hypermutation and class switch DNA recombination. Autoimmunity. 2009; 42:89–103.
   PubMed Web of Science ®Google Scholar
• Rush J. S., Liu M., Odegard V. H., Unniraman S., Schatz D. G.. Expression of activation-induced cytidine deaminase is regulated by cell division, providing a mechanistic basis for division-linked class switch recombination. Proc. Natl. Acad. Sci. USA. 2005; 102:13242–13247.
   PubMed Web of Science ®Google Scholar
• Rawlings D. J., Schwartz M. A., Jackson S. W., Meyer-Bahlburg A.. Integration of B cell responses through Toll-like receptors and antigen receptors. Nat. Rev. Immunol.. 2012; 12:282–294.
   PubMed Web of Science ®Google Scholar
• Zarnegar B., He J. Q., Oganesyan G., . Unique CD40-mediated biological program in B cell activation requires both type 1 and type 2 NF-κB activation pathways. Proc. Natl. Acad. Sci. USA. 2004; 101:8108–8113.
   PubMed Web of Science ®Google Scholar
• Park S. R., Zan H., Pal Z., . HoxC4 binds to the promoter of the cytidine deaminase AID gene to induce AID expression, class-switch DNA recombination and somatic hypermutation. Nat. Immunol.. 2009; 10:540–550.
   PubMed Web of Science ®Google Scholar
• Smale S. T.. Hierarchies of NF-κB target-gene regulation. Nat. Immunol.. 2011; 12:689–694.
   PubMed Web of Science ®Google Scholar
• Baltimore D.. NF-κB is 25. Nat. Immunol.. 2011; 12:683–685.
   PubMed Web of Science ®Google Scholar
• Sayegh C. E., Quong M. W., Agata Y., Murre C.. E-proteins directly regulate expression of activation-induced deaminase in mature B cells. Nat. Immunol.. 2003; 4:586–593.
   PubMed Web of Science ®Google Scholar
• Ise W., Kohyama M., Schraml B. U., . The transcription factor BATF controls the global regulators of class-switch recombination in both B cells and T cells. Nat. Immunol.. 2011; 12:536–543.
   PubMed Web of Science ®Google Scholar
• Pritchard C. C., Cheng H. H., Tewari M.. MicroRNA profiling: approaches and considerations. Nat. Rev. Genet.. 2012; 13:358–369.
   PubMed Web of Science ®Google Scholar
• Teng G., Hakimpour P., Landgraf P., . MicroRNA-155 is a negative regulator of activation-induced cytidine deaminase. Immunity. 2008; 28:621–629.
   PubMed Web of Science ®Google Scholar
• Dorsett Y., McBride K. M., Jankovic M., . MicroRNA-155 suppresses activation-induced cytidine deaminase-mediated Myc-IgH translocation. Immunity. 2008; 28:630–638.
   PubMed Web of Science ®Google Scholar
• de Yébenes V. G., Belver L., Pisano D. G., . miR-181b negatively regulates activation-induced cytidine deaminase in B cells. J. Exp. Med.. 2008; 205:2199–2206.
   PubMed Web of Science ®Google Scholar
• Borchert G. M., Holton N. W., Larson E. D.. Repression of human activation induced cytidine deaminase by miR-93 and miR-155. BMC Cancer. 2011; 10:347.
   Web of Science ®Google Scholar
• Basso K., Schneider C., Shen Q., . Bc16 positively regulates AID and germinal center gene expression via repression of miR-155. J. Exp. Med.. 2012; 209:2455–2465.
   PubMed Web of Science ®Google Scholar
• Thai T. H., Calado D. P., Casola S., . Regulation of the germinal center response by microRNA-155. Science. 2007; 316:604–608.
   PubMed Web of Science ®Google Scholar
• Landgraf P., Rusu M., Sheridan R., . A mammalian microRNA expression atlas based on small RNA library sequencing. Cell. 2007; 129:1401–1414.
   PubMed Web of Science ®Google Scholar
• Kluiver J., van den Berg A., de Jong D., . Regulation of pri-microRNA BIC transcription and processing in Burkitt lymphoma. Oncogene. 2007; 26:3769–3776.
   PubMed Web of Science ®Google Scholar
• Ito S., Nagaoka H., Shinkura R., . Activation-induced cytidine deaminase shuttles between nucleus and cytoplasm like apolipoprotein B mRNA editing catalytic polypeptide 1. Proc. Natl. Acad. Sci. USA. 2004; 101:1975–1980.
   PubMed Web of Science ®Google Scholar
• Cattoretti G., Buttner M., Shaknovich R., . Nuclear and cytoplasmic AID in extrafollicular and germinal center B cells. Blood. 2006; 107:3967–3975.
   PubMed Web of Science ®Google Scholar
• Pasqualucci L., Guglielmino R., Houldsworth J., . Expression of the AID protein in normal and neoplastic B cells. Blood. 2004; 104:3318–3325.
   PubMed Web of Science ®Google Scholar
• McBride K. M., Barreto V., Ramiro A. R., Stavropoulos P., Nussenzweig M. C.. Somatic hypermutation is limited by CRM1-dependent nuclear export of activation-induced deaminase. J. Exp. Med.. 2004; 199:1235–1244.
   PubMed Web of Science ®Google Scholar
• Brar S. S., Watson M., Diaz M.. Activation-induced cytosine deaminase (AID) is actively exported out of the nucleus but retained by the induction of DNA breaks. J. Biol. Chem.. 2004; 279:26395–26401.
   PubMed Web of Science ®Google Scholar
• Zaprazna K., Atchison M. L.. YY1 controls immunoglobulin class switch recombination and nuclear activation-induced deaminase levels. Mol. Cell. Biol.. 2012; 32:1542–1554.
   PubMed Web of Science ®Google Scholar
• Häsler J., Rada C., Neuberger M. S.. The cytoplasmic AID complex. Semin. Immunol.. 2012; 24:273–280.
   PubMedGoogle Scholar
• Orthwein A., Patenaude A. M., Affar el B., . Regulation of activation-induced deaminase stability and antibody gene diversification by Hsp90. J. Exp. Med.. 2010; 207:2751–2765.
   PubMed Web of Science ®Google Scholar
• Orthwein A., Zahn A., Methot S. P., . Optimal functional levels of activation-induced deaminase specifically require the Hsp40 DnaJa1. EMBO J.. 2011; 31:679–691.
   PubMedGoogle Scholar
• Chaudhuri J., Khuong C., Alt F. W.. Replication protein A interacts with AID to promote deamination of somatic hypermutation targets. Nature. 2004; 430:992–998.
   PubMed Web of Science ®Google Scholar
• Basu U., Chaudhuri J., Alpert C., . The AID antibody diversification enzyme is regulated by protein kinase A phosphorylation. Nature. 2005; 438:508–511.
   PubMedGoogle Scholar
• McBride K. M., Gazumyan A., Woo E. M., . Regulation of hypermutation by activation-induced cytidine deaminase phosphorylation. Proc. Natl. Acad. Sci. USA. 2006; 103:8798–8803.
   PubMed Web of Science ®Google Scholar
• Pasqualucci L., Kitaura Y., Gu H., Dalla-Favera R.. PKA-mediated phosphorylation regulates the function of activation-induced deaminase (AID) in B cells. Proc. Natl. Acad. Sci. USA. 2006; 103:395–400.
   PubMed Web of Science ®Google Scholar
• Ramiro A. R., Stavropoulos P., Jankovic M., Nussenzweig M. C.. Transcription enhances AID-mediated cytidine deamination by exposing single-stranded DNA on the nontemplate strand. Nat. Immunol.. 2003; 4:452–456.
   PubMed Web of Science ®Google Scholar
• Shinkura R., Tian M., Smith M., . The influence of transcriptional orientation on endogenous switch region function. Nat. Immunol.. 2003; 4:435–441.
   PubMed Web of Science ®Google Scholar
• Yu K., Chedin F., Hsieh C. L., Wilson T. E., Lieber M. R.. R-loops at immunoglobulin class switch regions in the chromosomes of stimulated B cells. Nat. Immunol.. 2003; 4:442–451.
   PubMed Web of Science ®Google Scholar
• Nambu Y., Sugai M., Gonda H., . Transcription-coupled events associating with immunoglobulin switch region chromatin. Science. 2003; 302:2137–2140.
   PubMed Web of Science ®Google Scholar
• Liu M., Duke J. L., Richter D. J., . Two levels of protection for the B cell genome during somatic hypermutation. Nature. 2008; 451:841–845.
   PubMed Web of Science ®Google Scholar
• Staszewski O., Baker R. E., Ucher A. J., . Activation-induced cytidine deaminase induces reproducible DNA breaks at many non-Ig Loci in activated B cells. Mol. Cell. 2011; 41:232–242.
   Google Scholar
• Klein I. A., Resch W., Jankovic M., . Translocation-capture sequencing reveals the extent and nature of chromosomal rearrangements in B lymphocytes. Cell. 2011; 147:95–106.
   PubMed Web of Science ®Google Scholar
• Chiarle R., Zhang Y., Frock R. L., . Genome-wide translocation sequencing reveals mechanisms of chromosome breaks and rearrangements in B cells. Cell. 2011; 147:107–119.
   PubMed Web of Science ®Google Scholar
• Xu Z., Fulop Z., Wu G., . 14-3-3 adaptor proteins recruit AID to 5′-AGCT-3′-rich switch regions for class switch recombination. Nature Struct. Mol. Biol.. 2010; 17:1124–1135.
   PubMed Web of Science ®Google Scholar
• Shen H. M., Poirier M. G., Allen M. J., . The activation-induced cytidine deaminase (AID) efficiently targets DNA in nucleosomes but only during transcription. J. Exp. Med.. 2009; 206:1057–1071.
   PubMedGoogle Scholar
• Conticello S. G., Ganesh K., Xue K., . Interaction between antibody-diversification enzyme AID and spliceosome-associated factor CTNNBL1. Mol. Cell. 2008; 31:474–484.
   PubMedGoogle Scholar
• Pavri R., Gazumyan A., Jankovic M., . Activation-induced cytidine deaminase targets DNA at sites of RNA polymerase II stalling by interaction with Spt5. Cell. 2010; 143:122–133.
   PubMed Web of Science ®Google Scholar
• Maeda K., Singh S. K., Eda K., . GANP-mediated recruitment of activation-induced cytidine deaminase to cell nuclei and to immunoglobulin variable region DNA. J. Biol. Chem.. 2010; 285:23945–23953.
   PubMedGoogle Scholar
• Okazaki I. M., Okawa K., Kobayashi M., . Histone chaperone Spt6 is required for class switch recombination but not somatic hypermutation. Proc. Natl. Acad. Sci. USA. 2011; 108:7920–7925.
   PubMedGoogle Scholar
• Nowak U., Matthews A. J., Zheng S., Chaudhuri J.. The splicing regulator PTBP2 interacts with the cytidine deaminase AID and promotes binding of AID to switch-region DNA. Nat. Immunol.. 2011; 12:160–166.
   PubMedGoogle Scholar
• Basu U., Meng F. L., Keim C., . The RNA exosome targets the AID cytidine deaminase to both strands of transcribed duplex DNA substrates. Cell. 2011; 144:353–363.
   PubMed Web of Science ®Google Scholar
• Stanlie A., Aida M., Muramatsu M., Honjo T., Begum N. A.. Histone3 lysine4 trimethylation regulated by the facilitates chromatin transcription complex is critical for DNA cleavage in class switch recombination. Proc. Natl. Acad. Sci. USA. 2010; 107:22190–22195.
   PubMed Web of Science ®Google Scholar
• Willmann K. L., Milosevic S., Pauklin S., . A role for the RNA pol II-associated PAF complex in AID-induced immune diversification. J. Exp. Med.. 2012; 209:2099–2111.
   PubMedGoogle Scholar
• Yamane A., Resch W., Kuo N., . Deep-sequencing identification of the genomic targets of the cytidine deaminase AID and its cofactor RPA in B lymphocytes. Nat. Immunol.. 2011; 12:62–69.
   PubMed Web of Science ®Google Scholar
• Xue K., Rada C., Neuberger M. S.. The in vivo pattern of AID targeting to immunoglobulin switch regions deduced from mutation spectra in msh2-/-ung-/-mice. J. Exp. Med.. 2006; 203:2085–2094.
   PubMed Web of Science ®Google Scholar
• Tafvizi A., Huang F., Fersht A. R., Mirny L. A., van Oijen A. M.. A single-molecule characterization of p53 search on DNA. Proc. Natl. Acad. Sci. USA. 2011; 108:563–568.
   Google Scholar
• Wang L., Wuerffel R., Feldman S., Khamlichi A. A., Kenter A. L.. S region sequence, RNA polymerase II, and histone modifications create chromatin accessibility during class switch recombination. J. Exp. Med.. 2009; 206:1817–1830.
   PubMed Web of Science ®Google Scholar
• Rajagopal D., Maul R. W., Ghosh A., . Immunoglobulin switch mu sequence causes RNA polymerase II accumulation and reduces dA hypermutation. J. Exp. Med.. 2009; 206:1237–1244.
   PubMed Web of Science ®Google Scholar
• Li, G., E. J. Pone, T. Mai, et al. 2012. Combinatorial H3K9acS10ph histone modifications target 14-3-3 adaptors and AID for class switch DNA recombination, Submitted.
   Google Scholar
• Li G., Zan H., Xu Z., Casali P.. Epigenetics of the antibody response. Trends Immunol.. 2012 In press.
   Google Scholar
• Jeevan-Raj B. P., Robert I., Heyer V., . Epigenetic tethering of AID to the donor switch region during immunoglobulin class switch recombination. J. Exp. Med.. 2011; 208:1649–1660.
   PubMed Web of Science ®Google Scholar
• Begum N. A., Stanlie A., Nakata M., Akiyama H., Honjo T.. The histone chaperone SPT6 is required for AID target determination through H3K4me3 regulation. J. Biol. Chem.. 2012; 287:32415–32429.
   PubMed Web of Science ®Google Scholar
• Fraenkel S., Mostoslavsky R., Novobrantseva T. I., . Allelic ‘choice’ governs somatic hypermutation in vivo at the immunoglobulin kappa-chain locus. Nat. Immunol.. 2007; 8:715–722.
   PubMed Web of Science ®Google Scholar
• Jolly C. J., Neuberger M. S.. Somatic hypermutation of immunoglobulin kappa transgenes: association of mutability with demethylation. Immunol. Cell Biol.. 2001; 79:18–22.
   PubMed Web of Science ®Google Scholar
• Larijani M., Frieder D., Sonbuchner T. M., . Methylation protects cytidines from AID-mediated deamination. Mol. Immunol.. 2005; 42:599–604.
   PubMedGoogle Scholar
• Odegard V. H., Kim S. T., Anderson S. M., Shlomchik M. J., Schatz D. G.. Histone modifications associated with somatic hypermutation. Immunity. 2005; 23:101–110.
   PubMed Web of Science ®Google Scholar
• Borchert G. M., Holton N. W., Edwards K. A., Vogel L. A., Larson E. D.. Histone H2A and H2B are monoubiquitinated at AID-targeted loci. PLoS One. 2010; 5:e11641.
   Google Scholar
• Vuong B. Q., Lee M., Kabir S., . Specific recruitment of protein kinase A to the immunoglobulin locus regulates class-switch recombination. Nat. Immunol.. 2009; 10:420–426.
   PubMedGoogle Scholar
• Golenser J., Domb A., Mordechai-Daniel T., . Iron chelators: correlation between effects on Plasmodium spp. and immune functions. J. Parasitol.. 2006; 92:170–177.
   PubMedGoogle Scholar
• Swingler S., Zhou J., Swingler C., . Evidence for a pathogenic determinant in HIV-1 Nef involved in B cell dysfunction in HIV/AIDS. Cell Host Microbe. 2008; 4:63–76.
   PubMedGoogle Scholar
• Barton J. C., Bertoli L. F., Acton R. T.. Common variable immunodeficiency and IgG subclass deficiency in central Alabama hemochromatosis probands homozygous for HFE C282Y. Blood Cells Mol. Dis.. 2003; 31:102–111.
   PubMedGoogle Scholar
• Watanabe-Matsui M., Muto A., Matsui T., . Heme regulates B-cell differentiation, antibody class switch, and heme oxygenase-1 expression in B cells as a ligand of Bach2. Blood. 2011; 117:5438–5448.
   PubMed Web of Science ®Google Scholar
• White C. A., Seth Hawkins J., Pone E. J., . AID dysregulation in lupus-prone MRL/Faslpr/lpr mice increases class switch DNA recombination and promotes interchromosomal c-Myc/IgH loci translocations: modulation by HoxC4. Autoimmunity. 2011; 44:585–598.
   PubMed Web of Science ®Google Scholar
• Hsu H. C., Wu Y., Yang P., . Overexpression of activation-induced cytidine deaminase in B cells is associated with production of highly pathogenic autoantibodies. J. Immunol.. 2007; 178:5357–5365.
   PubMed Web of Science ®Google Scholar
• Hsu H. C., Yang P., Wang J., . Interleukin 17-producing T helper cells and interleukin 17 orchestrate autoreactive germinal center development in autoimmune BXD2 mice. Nat. Immunol.. 2008; 9:166–175.
   PubMed Web of Science ®Google Scholar
• Hsu H. C., Yang P., Wu Q., . Inhibition of the catalytic function of activation-induced cytidine deaminase promotes apoptosis of germinal center B cells in BXD2 mice. Arthritis Rheum.. 2011; 63:2038–2048.
   PubMedGoogle Scholar
• Jiang C., Foley J., Clayton N., . Abrogation of lupus nephritis in activation-induced deaminase-deficient MRL/lpr mice. J. Immunol.. 2007; 178:7422–7431.
   PubMed Web of Science ®Google Scholar
• Jiang C., Zhao M. L., Diaz M.. Activation-induced deaminase heterozygous MRL/lpr mice are delayed in the production of high-affinity pathogenic antibodies and in the development of lupus nephritis. Immunology. 2009; 126:102–113.
   PubMed Web of Science ®Google Scholar
• Fish E. N.. The X-files in immunity: sex-based differences predispose immune responses. Nat. Rev. Immunol.. 2008; 8:737–744.
   PubMed Web of Science ®Google Scholar
• Klein S. L.. Immune cells have sex and so should journal articles. Endocrinology. 2012; 153:2544–2550.
   PubMed Web of Science ®Google Scholar
• Ackerman L. S.. Sex hormones and the genesis of autoimmunity. Arch. Dermatol.. 2006; 142:371–376.
   PubMedGoogle Scholar
• Pennock J. W., Stegall R., Bell B., . Estradiol improves genital herpes vaccine efficacy in mice. Vaccine. 2009; 27:5830–5836.
   PubMedGoogle Scholar
• Whitacre C. C.. Sex differences in autoimmune disease. Nat. Immunol.. 2001; 2:777–780.
   PubMed Web of Science ®Google Scholar
• Klein S. L., Jedlicka A., Pekosz A.. The Xs and Y of immune responses to viral vaccines. Lancet Infect Dis.. 2010; 10:338–349.
   PubMed Web of Science ®Google Scholar
• Cohen-Solal J. F., Jeganathan V., Hill L., . Hormonal regulation of B-cell function and systemic lupus erythematosus. Lupus. 2008; 17:528–532.
   PubMed Web of Science ®Google Scholar
• Fairweather D., Frisancho-Kiss S., Rose N. R.. Sex differences in autoimmune disease from a pathological perspective. Am. J. Pathol.. 2008; 173:600–609.
   PubMed Web of Science ®Google Scholar
• Cohen-Solal J. F., Jeganathan V., Grimaldi C. M., Peeva E., Diamond B.. Sex hormones and SLE: influencing the fate of autoreactive B cells. Curr. Top. Microbiol. Immunol.. 2006; 305:67–88.
   PubMedGoogle Scholar
• Grimaldi C. M.. Sex and systemic lupus erythematosus: the role of the sex hormones estrogen and prolactin on the regulation of autoreactive B cells. Curr. Opin. Rheumatol.. 2006; 18:456–461.
   PubMed Web of Science ®Google Scholar
• Lee T. P., Chiang B. L.. Sex differences in spontaneous versus induced animal models of autoimmunity. Autoimmun. Rev.. 2012; 11:A422–A429.
   PubMed Web of Science ®Google Scholar
• Heldring N., Pike A., Andersson S., . Estrogen receptors: how do they signal and what are their targets. Physiol. Rev.. 2007; 87:905–931.
   PubMed Web of Science ®Google Scholar
• Pauklin S., Sernandez I. V., Bachmann G., Ramiro A. R., Petersen-Mahrt S. K.. Estrogen directly activates AID transcription and function. J. Exp. Med.. 2009; 206:99–111.
   PubMed Web of Science ®Google Scholar
• Mai T., Zan H., Zhang J., . Estrogen receptors bind to and activate the promoter of the HoxC4 gene to potentiate HoxC4-mediated AID induction, immunoglobulin class-switch DNA recombination and somatic hypermutation. J. Biol. Chem.. 2010; 285:37797–37810.
   PubMed Web of Science ®Google Scholar
• McInnes I. B., Schett G.. The pathogenesis of rheumatoid arthritis. N. Engl. J. Med.. 2011; 365:2205–2219.
   PubMed Web of Science ®Google Scholar
• Xu X., Hsu H. C., Chen J., . Increased expression of activation-induced cytidine deaminase is associated with anti-CCP and rheumatoid factor in rheumatoid arthritis. Scand. J. Immunol.. 2009; 70:309–316.
   PubMed Web of Science ®Google Scholar
• Okazaki I. M., Hiai H., Kakazu N., . Constitutive expression of AID leads to tumorigenesis. J. Exp. Med.. 2003; 197:1173–1181.
   PubMed Web of Science ®Google Scholar
• Parsa J. Y., Basit W., Wang C. L., . AID mutates a non-immunoglobulin transgene independent of chromosomal position. Mol. Immunol.. 2007; 44:567–575.
   PubMedGoogle Scholar
• Feldhahn N., Henke N., Melchior K., . Activation-induced cytidine deaminase acts as a mutator in BCR-ABL1-transformed acute lymphoblastic leukemia cells. J. Exp. Med.. 2007; 204:1157–1166.
   PubMed Web of Science ®Google Scholar
• Nagaoka H., Tran T. H., Kobayashi M., Aida M., Honjo T.. Preventing AID, a physiological mutator, from deleterious activation: regulation of the genomic instability that is associated with antibody diversity. Int. Immunol.. 2010; 22:227–235.
   PubMed Web of Science ®Google Scholar
• Qin H., Suzuki K., Nakata M., . Activation-induced cytidine deaminase expression in CD4+T cells is associated with a unique IL-10-producing subset that increases with age. PLoS One. 2011; 6:e29141.
   PubMed Web of Science ®Google Scholar
• Rossi D., Berra E., Cerri M., . Aberrant somatic hypermutation in transformation of follicular lymphoma and chronic lymphocytic leukemia to diffuse large B-cell lymphoma. Haematologica. 2006; 91:1405–1409.
   PubMedGoogle Scholar
• Casellas R., Yamane A., Kovalchuk A. L., Potter M.. Restricting activation-induced cytidine deaminase tumorigenic activity in B lymphocytes. Immunology. 2009; 126:316–328.
   PubMedGoogle Scholar
• Klemm L., Duy C., Iacobucci I., . The B cell mutator AID promotes B lymphoid blast crisis and drug resistance in chronic myeloid leukemia. Cancer Cell. 2009; 16:232–245.
   PubMed Web of Science ®Google Scholar
• Strout M. P., Schatz D. G.. Imatinib resistance and progression of CML to blast crisis: somatic hypermutation AIDing the way. Cancer Cell. 2009; 16:174–176.
   PubMedGoogle Scholar
• Pérez-Durán P., de Yebenes V. G., Ramiro A. R.. Oncogenic events triggered by AID, the adverse effect of antibody diversification. Carcinogenesis. 2007; 28:2427–2433.
   PubMed Web of Science ®Google Scholar
• Okazaki I. M., Kotani A., Honjo T.. Role of AID in tumorigenesis. Adv. Immunol.. 2007; 94:245–273.
   PubMedGoogle Scholar
• Matsumoto Y., Marusawa H., Kinoshita K., . Up-regulation of activation-induced cytidine deaminase causes genetic aberrations at the CDKN2b-CDKN2a in gastric cancer. Gastroenterology. 2010; 139:1984–1994.
   PubMed Web of Science ®Google Scholar
• Endo Y., Marusawa H., Chiba T.. Involvement of activation-induced cytidine deaminase in the development of colitis-associated colorectal cancers. J. Gastroenterol.. 2011; 46 Suppl 1: 6–10.
   PubMedGoogle Scholar
• Shinmura K., Igarashi H., Goto M., . Aberrant expression and mutationinducing activity of AID in human lung cancer. Ann. Surg. Oncol.. 2011; 18:2084–2092.
   PubMed Web of Science ®Google Scholar
• Babbage G., Ottensmeier C. H., Blaydes J., Stevenson F. K., Sahota S. S.. Immunoglobulin heavy chain locus events and expression of activation-induced cytidine deaminase in epithelial breast cancer cell lines. Cancer Res.. 2006; 66:99–111.
   Google Scholar
• Macduff D. A., Neuberger M. S., Harris R. S.. MDM2 can interact with the C-terminus of AID but it is inessential for antibody diversification in DT40 B cells. Mol. Immunol.. 2006; 43:1099–1108.
   PubMedGoogle Scholar
• Demorest Z. L., MacDuff D. A., Brown W. L., . The interaction between AID and CIB1 is nonessential for antibody gene diversification by gene conversion or class switch recombination. PLoS One. 2010; 5:e11660.
   PubMedGoogle Scholar