ArticleProceedings of the National Academy of Sciences of the United States of America2009
Carboxy-terminal domain of AID required for its mRNA complex formation in vivo.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
- B-Cell Epigenetic Modulation of IgA Response by 5-Azacytidine and IgA Nephropathy.Journal of the American Society of Nephrology : JASN · 2024Article
- RNA 2'-O-methylation promotes persistent R-loop formation and AID-mediated IgH class switch recombination.BMC biology · 2024Article
- Ago2 and a miRNA reduce Topoisomerase 1 for enhancing DNA cleavage in antibody diversification by activation-induced cytidine deaminase.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- C-terminal deletion-induced condensation sequesters AID from IgH targets in immunodeficiency.The EMBO journal · 2022Article
- Review
- The APOBEC Protein Family: United by Structure, Divergent in Function.Trends in biochemical sciences · 2016Review
- C-terminal region of activation-induced cytidine deaminase (AID) is required for efficient class switch recombination and gene conversion.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- A comprehensive analysis of the effects of the deaminase AID on the transcriptome and methylome of activated B cells.Nature immunology · 2013Article
- RNA editing of hepatitis B virus transcripts by activation-induced cytidine deaminase.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Functions and regulation of the APOBEC family of proteins.Seminars in cell & developmental biology · 2012Review
- LINE-1 retroelements complexed and inhibited by activation induced cytidine deaminase.PloS one · 2012Article
- Epigenetic tethering of AID to the donor switch region during immunoglobulin class switch recombination.The Journal of experimental medicine · 2011Article
- Histone chaperone Spt6 is required for class switch recombination but not somatic hypermutation.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- A coming-of-age story: activation-induced cytidine deaminase turns 10.Nature immunology · 2009Review
- The C-terminal region of activation-induced cytidine deaminase is responsible for a recombination function other than DNA cleavage in class switch recombination.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Activation-induced cytidine deaminase (AID) is essential for the class switch recombination (CSR) and somatic hypermutation (SHM) of Ig genes. Originally, AID was postulated to be an RNA-editing enzyme, because of its structural homology with a known RNA-editing enzyme, APOBEC1. In support of this idea, AID shares many of the properties of RNA-editing enzymes, including nucleocytoplasmic shuttling and a dependency on de novo protein synthesis. However, it has not been shown whether AID recognizes a specific mRNA and edits it to generate an enzyme involved in CSR or SHM. Here, we examined the association between AID and polyadenylated [poly(A)(+)] RNA in vivo, using UV cross-linking coupled with a poly(A) capture method that relies on biotinylated oligo(dT) and streptavidin-conjugated beads. We found that both exogenous AID expressed in transfected CH12 cells and endogenous AID expressed in BL2 cells were associated with poly(A)(+) RNA. Similar protein-poly(A)(+) RNA complexes were formed by APOBEC1 and APOBEC3G. However, the interactions of all of these cytidine deaminase family members, including AID, with poly(A)(+) RNA were indirect. This was expected for APOBEC1, which is known to act through an RNA-interacting cofactor, APOBEC1 complementation factor (ACF). In addition, the carboxy-terminal region of AID, which is essential for class switching, was also required for its interaction with poly(A)(+) RNA. These results suggest that the CSR activity of AID requires an ACF-like cofactor that specifically interacts with the carboxy-terminal domain of AID.
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