Biochemistry (Moscow)

, Volume 84, Issue 8, pp 896–904 | Cite as

RNA Editing by ADAR Adenosine Deaminases: From Molecular Plasticity of Neural Proteins to the Mechanisms of Human Cancer

  • A. O. Goncharov
  • A. A. Kliuchnikova
  • S. S. Nasaev
  • S. A. MoshkovskiiEmail author


RNA editing by adenosine deaminases of the ADAR family attracts a growing interest of researchers, both zoologists studying ecological and evolutionary plasticity of invertebrates and medical biochemists focusing on the mechanisms of cancer and other human diseases. These enzymes deaminate adenosine residues in the double-stranded (ds) regions of RNA with the formation of inosine. As a result, some RNAs change their three-dimensional structure and functions. Adenosine-to-inosine editing in the mRNA coding sequences may cause amino acid substitutions in the encoded proteins. Here, we reviewed current concepts on the functions of two active ADAR isoforms identified in mammals (including humans). The ADAR1 protein, which acts non-specifically on extended dsRNA regions, is capable of immunosuppression via inactivation of the dsRNA interactions with specific sensors inducing the cell immunity. Expression of a specific ADAR1 splicing variant is regulated by the type I interferons by the negative feedback mechanism. It was shown that immunosuppressing effects of ADAR1 facilitate progression of some types of cancer. On the other hand, changes in the amino acid sequences resulting from the mRNA editing by the ADAR enzymes can result in the formation of neoantigens that can activate the antitumor immunity. The ADAR2 isoform acts on RNA more selectively; its function is associated with the editing of mRNA coding regions and can lead to the amino acid substitutions, in particular, those essential for the proper functioning of some neurotransmitter receptors in the central nervous system.


adenosine deaminase RNA editing ADAR cancer immunity neoantigen 



adenosine deaminase, RNA-dependent


double-stranded RNA


protein kinase R


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Funding. This work is supported by the Russian Science Foundation (project no. 17-15-01229).

Conflict of interest. The authors declare no conflict of interest in financial of any other sphere.

Ethical approval. This paper contains no studies using animal or human subjects.


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Copyright information

© Pleiades Publishing, Ltd. 2019

Authors and Affiliations

  • A. O. Goncharov
    • 1
  • A. A. Kliuchnikova
    • 1
    • 2
  • S. S. Nasaev
    • 2
  • S. A. Moshkovskii
    • 1
    • 2
    Email author
  1. 1.Institute of Biomedical ChemistryMoscowRussia
  2. 2.Pirogov Russian National Research Medical UniversityMoscowRussia

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