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Summary: Review
Post-translational regulation of
activation-induced cytidine deaminase
Uttiya Basu1,2,3
, Andrew Franklin1,2,3
and Frederick W. Alt1,2,3,*
1
Howard Hughes Medical Institute, The Children's Hospital, Boston, MA 02115, USA
2
Department of Genetics, Harvard Medical School, Boston, MA 02115, USA
3
Immune Disease Institute, Boston, MA 02115, USA
The assembled immunoglobulin genes in the B cells of mice and humans are altered by distinct
processes known as class switch recombination (CSR) and somatic hypermutation, leading to
diversification of the antibody repertoire. These two DNA modification processes are initiated by the
B cell-specific protein factor activation-induced cytidine deaminase (AID). AID is post-
translationally modified by phosphorylation at multiple sites, although functional significance
during CSR has been implicated only for phosphorylation at serine-38 (S38). Although multiple
laboratories have demonstrated that AID function is regulated via phosphorylation at S38, the
precise biological role of S38 phosphorylation has been a topic of debate. Here, we discuss our
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