{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T05:25:34Z","timestamp":1777353934026,"version":"3.51.4"},"reference-count":60,"publisher":"Proceedings of the National Academy of Sciences","issue":"23","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2006,6,6]]},"abstract":"<jats:p>\n                    Activation-induced cytidine deaminase (AID) initiates Ig class switch recombination and somatic hypermutation by producing U:G mismatches in DNA. These mismatches also have the potential to induce DNA damage including double-stranded breaks and chromosome translocations; therefore, strict regulation of AID is important for maintaining genomic stability. In addition to transcriptional regulation, it has been proposed that phosphorylation can also modulate AID activity. Using a combination of MS and immunochemical approaches we found that 5\u201315% of the AID expressed in activated B cells was phosphorylated at serine-38 (p38AID). This form of AID was enriched in the chromatin fraction in activated B cells, suggesting a role for phosphorylation in targeting AID to DNA. Consistent with this idea, serine-38 to alanine mutant AID (AID\n                    <jats:sup>S38A<\/jats:sup>\n                    ) showed diminished somatic hypermutation activity on artificial and physiological DNA targets. We conclude that a small fraction of AID is phosphorylated in activated B cells and that the modified form contributes disproportionately to hypermutation.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0603272103","type":"journal-article","created":{"date-parts":[[2006,5,24]],"date-time":"2006-05-24T20:36:00Z","timestamp":1148502960000},"page":"8798-8803","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":123,"title":["Regulation of hypermutation by activation-induced cytidine deaminase phosphorylation"],"prefix":"10.1073","volume":"103","author":[{"given":"Kevin M.","family":"McBride","sequence":"first","affiliation":[{"name":"*Laboratory of Molecular Immunology and"}]},{"given":"Anna","family":"Gazumyan","sequence":"additional","affiliation":[{"name":"*Laboratory of Molecular Immunology and"},{"name":"Howard Hughes Medical Institute, New York, NY 10021"}]},{"given":"Eileen M.","family":"Woo","sequence":"additional","affiliation":[{"name":"Laboratory of Mass Spectrometry, The Rockefeller University and"}]},{"given":"Vasco M.","family":"Barreto","sequence":"additional","affiliation":[{"name":"*Laboratory of Molecular Immunology and"}]},{"given":"Davide F.","family":"Robbiani","sequence":"additional","affiliation":[{"name":"*Laboratory of Molecular Immunology and"}]},{"given":"Brian T.","family":"Chait","sequence":"additional","affiliation":[{"name":"Laboratory of Mass Spectrometry, The Rockefeller University and"}]},{"given":"Michel C.","family":"Nussenzweig","sequence":"additional","affiliation":[{"name":"*Laboratory of Molecular Immunology and"},{"name":"Howard Hughes Medical Institute, New York, NY 10021"}]}],"member":"341","published-online":{"date-parts":[[2006,6,6]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1038\/302575a0"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.81.10.3180"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1038\/381751a0"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.274.26.18470"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)00078-7"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)00079-9"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0730835100"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature01574"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature00981"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.20030481"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature00862"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1038\/ni920"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature01760"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0960-9822(02)01215-0"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.molcel.2004.10.011"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1038\/ni974"},{"key":"e_1_3_3_17_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.191.3.579"},{"key":"e_1_3_3_18_2","doi-asserted-by":"crossref","first-page":"3121","DOI":"10.4049\/jimmunol.162.6.3121","volume":"162","author":"Phung Q. 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