Please use this identifier to cite or link to this item: https://doi.org/10.1093/nar/gky348
Title: Tissue-selective restriction of RNA editing of CaV1.3 by splicing factor SRSF9
Authors: Huang, H. 
Kapeli, K. 
Jin, W. 
Wong, Y.P. 
Arumugam, T.V. 
Koh, J.H. 
Srimasorn, S. 
Mallilankaraman, K. 
En Chua, J.J. 
Yeo, G.W. 
Soong, T.W. 
Issue Date: 2018
Publisher: Oxford University Press
Citation: Huang, H., Kapeli, K., Jin, W., Wong, Y.P., Arumugam, T.V., Koh, J.H., Srimasorn, S., Mallilankaraman, K., En Chua, J.J., Yeo, G.W., Soong, T.W. (2018). Tissue-selective restriction of RNA editing of CaV1.3 by splicing factor SRSF9. Nucleic Acids Research 46 (14) : 7323-7338. ScholarBank@NUS Repository. https://doi.org/10.1093/nar/gky348
Rights: Attribution-NonCommercial 4.0 International
Abstract: Adenosine DeAminases acting on RNA (ADAR) catalyzes adenosine-to-inosine (A-to-I) conversion within RNA duplex structures. While A-to-I editing is often dynamically regulated in a spatialtemporal manner, the mechanisms underlying its tissue-selective restriction remain elusive. We have previously reported that transcripts of voltage-gated calcium channel CaV1.3 are subject to brain-selective A-to-I RNA editing by ADAR2. Here, we show that editing of CaV1.3 mRNA is dependent on a 40 bp RNA duplex formed between exon 41 and an evolutionarily conserved editing site complementary sequence (ECS) located within the preceding intron. Heterologous expression of a mouse minigene that contained the ECS, intermediate intronic sequence and exon 41 with ADAR2 yielded robust editing. Interestingly, editing of CaV1.3 was potently inhibited by serine/arginine-rich splicing factor 9 (SRSF9). Mechanistically, the inhibitory effect of SRSF9 required direct RNA interaction. Selective down-regulation of SRSF9 in neurons provides a basis for the neuronspecific editing of CaV1.3 transcripts. © 2018 Oxford University Press. All Rights Reserved.
Source Title: Nucleic Acids Research
URI: https://scholarbank.nus.edu.sg/handle/10635/210868
ISSN: 03051048
DOI: 10.1093/nar/gky348
Rights: Attribution-NonCommercial 4.0 International
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