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Specific Expression of Activation-induced Cytidine Deaminase (AID), a Novel Member of the RNA-editing Deaminase Family in Germinal Center B Cells*
TLDR
Findings suggest that AID is a new member of the RNA-editing deaminase family and may play a role in genetic events in the germinal center B cell.
Molecular mechanism of class switch recombination: linkage with somatic hypermutation.
TLDR
Class switch recombination and somatic hypermutation have been considered to be mediated by different molecular mechanisms, but involvement of activation-induced cytidine deaminase in both CSR and SHM has revealed that the two genetic alteration mechanisms are surprisingly similar.
Aberrant expansion of segmented filamentous bacteria in IgA-deficient gut
TLDR
The results indicate that secretions of IgAs rather than innate defense peptides are critical to regulation of commensal bacterial flora and that the segmented filamentous bacteria antigens are strong stimuli of the mucosal immune system.
AID is required to initiate Nbs1/γ-H2AX focus formation and mutations at sites of class switching
TLDR
It is reported that the Nijmegen breakage syndrome protein and phosphorylated H2A histone family member X (γ-H2AX) form nuclear foci at the Ch region in the G1 phase of the cell cycle in cells undergoing CSR, and that switching is impaired in H2AX-/- mice.
AID mutant analyses indicate requirement for class-switch-specific cofactors
TLDR
It is reported that human AID mutant proteins with insertions, replacements or truncations in the C-terminal region retained strong SHM activity but almost completely lost CSR activity, indicating that AID requires interaction with a cofactor(s) specific to CSR.
In situ class switching and differentiation to IgA-producing cells in the gut lamina propria
TLDR
It is concluded that IgA+ cells in the gut lamina propria are generated in situ from B220+IgM+ lymphocytes, as they still express both AID and transcripts from circular DNA that has been ‘looped-out' during CSR.
Activation-induced cytidine deaminase shuttles between nucleus and cytoplasm like apolipoprotein B mRNA editing catalytic polypeptide 1
TLDR
It is demonstrated that AID is a nucleocytoplasmic shuttling protein with a bipartite nuclear localization signal and a nuclear export signal in its N and C termini, respectively, suggesting that both AID and ApoB100 may have homologous reaction mechanisms.
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