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- W2779169037 abstract "Activation-induced cytidine deaminase (AID) is a mutator enzyme that targets immunoglobulin (Ig) genes to initiate antibody somatic hypermutation (SHM) and class switch recombination (CSR). Off-target AID association also occurs, which causes oncogenic mutations and chromosome rearrangements. However, AID occupancy does not directly correlate with DNA damage, suggesting that factors beyond AID association contribute to mutation targeting. CSR and SHM are regulated by phosphorylation on AID serine38 (pS38), but the role of pS38 in off-target activity has not been evaluated. We determined that lithium, a clinically used therapeutic, induced high AID pS38 levels. Using lithium and an AID-S38 phospho mutant, we compared the role of pS38 in AID activity at the Ig switch region and off-target Myc gene. We found that deficient pS38 abated AID chromatin association and CSR but not mutation at Myc. Enhanced pS38 elevated Myc translocation and mutation frequency but not CSR or Ig switch region mutation. Thus, AID activity can be differentially targeted by phosphorylation to induce oncogenic lesions." @default.
- W2779169037 created "2018-01-05" @default.
- W2779169037 creator A5067565454 @default.
- W2779169037 creator A5068250768 @default.
- W2779169037 creator A5091882153 @default.
- W2779169037 date "2017-11-09" @default.
- W2779169037 modified "2023-10-05" @default.
- W2779169037 title "Phosphorylation promotes activation-induced cytidine deaminase activity at the Myc oncogene" @default.
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- W2779169037 doi "https://doi.org/10.1084/jem.20170468" @default.
- W2779169037 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5716038" @default.
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- W2779169037 hasPublicationYear "2017" @default.
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