ArticleScientific reports2019
Protein kinase A inhibits tumor mutator APOBEC3B through phosphorylation.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Effects of thymidylate synthase inhibitors differ in genomic uracilation and mutagenic potential.Life science alliance · 2026Article
- Isolation, biochemical characterization, and primary structure and active site determination ofBiochemistry and biophysics reports · 2025Article
- APOBEC3B Does Not Promote Tumor Progression in Tp53 Hemizygous Mice.Cancer reports (Hoboken, N.J.) · 2025Article
- Alternative Splicing, RNA Editing, and the Current Limits of Next Generation Sequencing.Genes · 2023Article
- The APOBEC3B cytidine deaminase is an adenovirus restriction factor.PLoS pathogens · 2023Article
- APOBEC mutagenesis, kataegis, chromothripsis in EGFR-mutant osimertinib-resistant lung adenocarcinomas.Annals of oncology : official journal of the European Society for Medical Oncology · 2022Article
- ILF2 enhances the DNA cytosine deaminase activity of tumor mutator APOBEC3B in multiple myeloma cells.Scientific reports · 2022Article
- Review
- Review
- Identification of a Novel Cis-Acting Regulator of HIV-1 Genome Packaging.International journal of molecular sciences · 2021Article
- CancerFrontiers in immunology · 2021Article
- Molecular origins of APOBEC-associated mutations in cancer.DNA repair · 2020Review
- Molecular basis of clonal evolution in multiple myeloma.International journal of hematology · 2020Review
- APOBEC3A is a prominent cytidine deaminase in breast cancer.PLoS genetics · 2019Article
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Authors and funding
17 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
APOBEC3B cytidine deaminase (A3B) catalyzes cytosine into uracil in single-strand DNA and induces C-to-T mutations in genomic DNA of various types of tumors. Accumulation of APOBEC signature mutations is correlated with a worse prognosis for patients with breast cancer or multiple myeloma, suggesting that A3B activity might be a cause of the unfavorable DNA mutations and clonal evolution in these tumors. Phosphorylation of conserved threonine residues of other cytidine deaminases, activation induced deaminase (AID) and APOBEC3G, inhibits their activity. Here we show that protein kinase A (PKA) physically binds to A3B and phosphorylates Thr214. In vitro deaminase assays and foreign DNA editing assays in cells confirm that phosphomimetic A3B mutants, T214D and T214E, completely lose deaminase activity. Molecular dynamics simulation of A3B phosphorylation reveals that Thr214 phosphorylation disrupts binding between the phospho-A3B catalytic core and ssDNA. These mutants still inhibit retroviral infectivity at least partially, and also retain full anti-retrotransposition activity. These results imply that PKA-mediated phosphorylation inhibits A3B mutagenic activity without destructing its innate immune functions. Therefore, PKA activation could reduce further accumulation of mutations in A3B overexpressing tumors.
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