title: Post-translational regulation of activation-induced cytidine deaminase.
abstract: 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 interpretation of the significance of AID regulation via phosphorylation and also discuss how this form of AID regulation may have evolved in higher organisms.
authors.affiliation: Howard Hughes Medical Institute, The Children's Hospital, Boston, MA 02115, USA.
authors.forename: Uttiya
authors.initials: U
authors.lastname: Basu
authors.forename: Andrew
authors.initials: A
authors.lastname: Franklin
authors.forename: Frederick W
authors.initials: FW
authors.lastname: Alt
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D003564:Cytidine Deaminase / Q000235:genetics / Q000378:metabolism*; D004789:Enzyme Activation; D017578:Immunoglobulin Class Switching / Q000235:genetics*; D008954:Models, Biological; D008969:Molecular Sequence Data; D010766:Phosphorylation; D027041:Somatic Hypermutation, Immunoglobulin / Q000235:genetics*; D015027:Zebrafish
chemical_list: D003564:Cytidine Deaminase