December 2025 - Vinod Rajendra

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Dr. Vinod Rajendra

MedUni Wien RESEARCHER OF THE MONTH December 2025

Adenosine-to-inosine (A-to-I) RNA editing is catalyzed by ADAR enzymes in double-stranded RNA regions. ADAR1 drives most editing events in humans. Although ADAR1 is thought to function as a homodimer, the structural basis and functional consequences of dimerization have remained elusive. In this study, we present the structure of the third dsRNA-binding domain (dsRBD3) of ADAR1, revealing stable dimer formation via a large interface. Using this insight, we generated a mutant that disrupts dimerization. Interestingly, loss of dimerization did not abolish editing activity but selectively altered editing efficiency at specific sites, highlighting a nuanced role for dimerization in site selection and offering a new angle for modulating ADAR1 function.

Selected Literature

1. Kleinova, R., et al., The ADAR1 editome reveals drivers of editing-specificity for ADAR1-isoforms. Nucleic Acids Res, 2023. 51(9): p. 4191-4207.

2. Goldeck, M.Rajendra,V., et al., How RNA editing keeps an I on physiology. Am J Physiol Cell Physiol, 2022. 323(5): p. C1496-C1511.

3. Mboukou, A.Rajendra, V., et al., Transportin-1: A Nuclear Import Receptor with Moonlighting Functions. Front Mol Biosci, 2021. 8: p. 638149.

4. Sahu, U. Rajendra, V., et al., Methionine synthase is localized to the nucleus in Pichia pastoris and Candida albicans and to the cytoplasm in Saccharomyces cerevisiae. J Biol Chem, 2017. 292(36): p. 14730-14746.

5. Mboukou, A.Rajendra, V., et al., Dimerization of ADAR1 modulates site-specificity of RNA editing. Nat Commun, 2024. 15(1): p. 10051.

6. Bormann D, Copic D, Klas K, Direder M, Riedl CJ, Testa G, et al. Exploring the heterogeneous transcriptional response of the CNS to systemic LPS and Poly(I:C). Neurobiol Dis. 2023;188:106339.