APOBEC1

Last update 08 May 2025

Basic Info

Synonyms

APOBEC-1, APOBEC1, apolipoprotein B mRNA editing enzyme catalytic subunit 1

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Introduction

Cytidine deaminase catalyzing the cytidine to uridine postranscriptional editing of a variety of mRNAs (PubMed:30844405). Form complexes with cofactors that confer differential editing activity and selectivity. Responsible for the postranscriptional editing of a CAA codon for Gln to a UAA codon for stop in the apolipoprotein B mRNA (PubMed:24916387). Also involved in CGA (Arg) to UGA (Stop) editing in the NF1 mRNA (PubMed:11727199). May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation (By similarity).

100 Clinical Results associated with APOBEC1

100 Translational Medicine associated with APOBEC1

0 Patents (Medical) associated with APOBEC1

425

Literatures (Medical) associated with APOBEC1

01 Mar 2025·Cancer Science

Spatial immune heterogeneity in a mouse tumor model after immunotherapy

Article

Author: Nunvar, Jaroslav ; Smahel, Michal ; Pfeiferova, Lucie ; Johari, Shweta Dilip ; Smahelova, Jana

AbstractCancer immunotherapy is increasingly used in clinical practice, but its success rate is reduced by tumor escape from the immune system. This may be due to the genetic instability of tumor cells, which allows them to adapt to the immune response and leads to intratumoral immune heterogeneity. The study investigated spatial immune heterogeneity in the tumor microenvironment and its possible drivers in a mouse model of tumors induced by human papillomaviruses (HPV) following immunotherapy. Gene expression was determined by RNA sequencing and mutations by whole exome sequencing. A comparison of different tumor areas revealed heterogeneity in immune cell infiltration, gene expression, and mutation composition. While the mean numbers of mutations with every impact on gene expression or protein function were comparable in treated and control tumors, mutations with high or moderate impact were increased after immunotherapy. The genes mutated in treated tumors were significantly enriched in genes associated with ECM metabolism, degradation, and interactions, HPV infection and carcinogenesis, and immune processes such as antigen processing and presentation, Toll‐like receptor signaling, and cytokine production. Gene expression analysis of DNA damage and repair factors revealed that immunotherapy upregulated Apobec1 and Apobec3 genes and downregulated genes related to homologous recombination and translesion synthesis. In conclusion, this study describes the intratumoral immune heterogeneity, that could lead to tumor immune escape, and suggests the potential mechanisms involved.

01 Mar 2025·Molecular Cell

Single-molecule m6A detection empowered by endogenous labeling unveils complexities across RNA isoforms

Article

Author: Liu, Jiayin ; Zhang, Jie ; Huang, Xiang ; Wei, Chuanchuan ; Guo, Yang ; Wang, Jinkai ; Guo, Wenbing ; Zhang, Zijun ; Cun, Yixian ; Wu, Zehong ; He, Jialiang ; Ren, Zhijun ; Shao, Jingwen ; He, Jianbo ; Feng, Zhengming ; Ma, Xiaojun

The landscape of N⁶-methyadenosine (m⁶A) on different RNA isoforms is still incompletely understood. Here, in HEK293T cells, we endogenously label the methylated m⁶A sites on single Oxford Nanopore Technology (ONT) direct RNA sequencing (DRS) reads by APOBEC1-YTH-induced C-to-U mutations 10-100 nt away, obtaining 1,020,237 5-mer single-read m⁶A signals. We then trained m6Aiso, a deep residual neural network model that accurately identifies and quantifies m⁶A at single-read resolution. Analyzing m6Aiso-determined m⁶A on single reads and isoforms uncovers distance-dependent linkages of m⁶A sites along single molecules. It also uncovers specific methylation of identical m⁶A sites on intron-retained isoforms, partly due to their differential distances to exon junctions and isoform-specific binding of TARBP2. Moreover, we find that transcription factor SMAD3 promotes m⁶A deposition on its transcribed RNA isoforms during epithelial-mesenchymal transition, resulting in isoform-specific regulation of m⁶A on isoforms with alternative promoters. Our study underscores the effectiveness of m6Aiso in elucidating the intricate dynamics and complexities of m⁶A across RNA isoforms.

25 Feb 2025·Journal of Virology

APOBEC-1 cofactors regulate APOBEC3-induced mutations in hepatitis B virus

Article

Author: Patterson, Amy P. ; Chen, Zhigang ; Bocharov, Alexander V. ; Vishnyakova, Tatyana G. ; Baranova, Irina N. ; Eggerman, Thomas L.

ABSTRACTAPOBEC3 proteins (A3s) play an important role in host innate immunity against viruses and DNA mutations in cancer. A3s-induced mutations in both viral and human DNA genomes vary significantly from non-lethal mutations in viruses to localized hypermutations, such as kataegis in cancer. How A3s are regulated remains largely unknown. Since A3s exist in complexes and belong to the same family as APOBEC-1 (A1), which requires cofactors to be functional, we investigated the role of A1 cofactors and other A3 potentially associated hnRNPs on A3 mutational activity using hepatitis B virus (HBV) cellular replication as a model. We found that A1-associated cofactors and other hnRNPs were involved in A3 mutational activity regulation, and their regulatory effect was dependent on the strength of A3 association with hnRNPs with an order of A3C > 3G>3B and A1 cofactors > other hnRNPs. A1 cofactors had a strong protein interaction with A3 and significantly increased A3 mutational activity by co-expression. Endogenous gene expression knockdown by siRNA had the opposite decrease effect. Disruption of the protein interactions between A3 and hnRNPs through A3G and A3B mutagenesis decreased A3 mutational activity significantly, even to a level of near total loss, indicating that A1 cofactors and hnRNPs are required for A3 mutational activity. HBV genome-wide mutation analyses showed that A1 cofactors significantly increased A3C accessibility to HBV (−)DNA and A3C-induced mutational efficiency to generate kataegis-like hypermutation. These data demonstrate that A1 cofactors and hnRNPs are closely associated with A3s and may play an important regulatory role under physiological conditions.IMPORTANCEAs human host restriction factors, A3s play an important role against viral infections. A3s are also major mutagenic drivers of cancer. However, why A3-induced mutations vary significantly from non-lethal mutations in virus to localized hypermutations in cancer remains unknown. We found that A1 cofactor and other hnRNPs are not only associated with A3 complexes but also play important regulatory roles in A3-induced mutation activities. A1 cofactors like GRY-RBP significantly increased A3 accessibility and mutational efficiency to its single-strand DNA substrate during HBV reverse transcription to generate hypermutations. Disruption of the A3 protein association with hnRNPs by A3 mutagenesis diminished A3 mutational activity. This finding not only reveals a regulatory mechanism for A3-induced mutation but also indicates that A3-associated cellular factors can be a potential target for regulating A3-induced mutation for cancer therapeutics.

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APOBEC1

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