Tissue-selective restriction of RNA editing of CaV1.3 by splicing factor SRSF9
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 spatial-temporal manner, the mechanisms underlying its tissue-selective restriction remain elusive. We have pre...
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| Published in | Nucleic acids research Vol. 46; no. 14; pp. 7323 - 7338 |
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| Main Authors | , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
England
Oxford University Press
21.08.2018
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| Abstract | 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 spatial-temporal 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 neuron-specific editing of CaV1.3 transcripts. |
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| AbstractList | 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 spatial-temporal 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 neuron-specific editing of CaV1.3 transcripts. 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 spatial-temporal 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 neuron-specific editing of CaV1.3 transcripts. 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 spatial-temporal 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 neuron-specific editing of CaV1.3 transcripts.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 spatial-temporal 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 neuron-specific editing of CaV1.3 transcripts. 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 spatial-temporal manner, the mechanisms underlying its tissue-selective restriction remain elusive. We have previously reported that transcripts of voltage-gated calcium channel Ca V 1.3 are subject to brain-selective A-to-I RNA editing by ADAR2. Here, we show that editing of Ca V 1.3 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 Ca V 1.3 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 neuron-specific editing of Ca V 1.3 transcripts. |
| Author | Kapeli, Katannya Arumugam, Thiruma Valavan Srimasorn, Sumitra Chua, John Jia En Mallilankaraman, Karthik Wong, Yuk Peng Koh, Joanne Huifen Soong, Tuck Wah Yeo, Gene W Huang, Hua Jin, Wenhao |
| AuthorAffiliation | 2 Neurobiology/Ageing Programme, Life Sciences Institute, National University of Singapore, Singapore 117456, Singapore 4 Department of Cellular and Molecular Medicine, Stem Cell Program and Institute for Genomic Medicine, University of California, San Diego, La Jolla, USA 1 Department of Physiology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597, Singapore 3 Institute of Molecular and Cell Biology, Agency for Science, Technology and Research (ASTAR), Singapore 138673, Singapore 5 Molecular Engineering Laboratory, ASTAR, Singapore, Singapore |
| AuthorAffiliation_xml | – name: 3 Institute of Molecular and Cell Biology, Agency for Science, Technology and Research (ASTAR), Singapore 138673, Singapore – name: 4 Department of Cellular and Molecular Medicine, Stem Cell Program and Institute for Genomic Medicine, University of California, San Diego, La Jolla, USA – name: 2 Neurobiology/Ageing Programme, Life Sciences Institute, National University of Singapore, Singapore 117456, Singapore – name: 5 Molecular Engineering Laboratory, ASTAR, Singapore, Singapore – name: 1 Department of Physiology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597, Singapore |
| Author_xml | – sequence: 1 givenname: Hua surname: Huang fullname: Huang, Hua email: phshhua@nus.edu.sg organization: Department of Physiology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597, Singapore – sequence: 2 givenname: Katannya surname: Kapeli fullname: Kapeli, Katannya organization: Department of Physiology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597, Singapore – sequence: 3 givenname: Wenhao surname: Jin fullname: Jin, Wenhao organization: Department of Physiology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597, Singapore – sequence: 4 givenname: Yuk Peng surname: Wong fullname: Wong, Yuk Peng organization: Department of Physiology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597, Singapore – sequence: 5 givenname: Thiruma Valavan surname: Arumugam fullname: Arumugam, Thiruma Valavan organization: Department of Physiology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597, Singapore – sequence: 6 givenname: Joanne Huifen surname: Koh fullname: Koh, Joanne Huifen organization: Department of Physiology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597, Singapore – sequence: 7 givenname: Sumitra surname: Srimasorn fullname: Srimasorn, Sumitra organization: Department of Physiology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597, Singapore – sequence: 8 givenname: Karthik surname: Mallilankaraman fullname: Mallilankaraman, Karthik organization: Department of Physiology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597, Singapore – sequence: 9 givenname: John Jia En surname: Chua fullname: Chua, John Jia En organization: Department of Physiology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597, Singapore – sequence: 10 givenname: Gene W surname: Yeo fullname: Yeo, Gene W organization: Department of Physiology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597, Singapore – sequence: 11 givenname: Tuck Wah surname: Soong fullname: Soong, Tuck Wah email: phsstw@nus.edu.sg organization: Department of Physiology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597, Singapore |
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Adenosine DeAminases acting on RNA (ADAR) catalyzes adenosine-to-inosine (A-to-I) conversion within RNA duplex structures. While A-to-I editing is... 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... |
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| SubjectTerms | Adenosine Deaminase - genetics Adenosine Deaminase - metabolism Animals Base Sequence Calcium Channels, L-Type - genetics Calcium Channels, L-Type - metabolism Cell Line, Tumor Cells, Cultured Gene Expression Regulation HEK293 Cells Humans Kidney - metabolism Mice, Inbred C57BL Organ Specificity - genetics Rats RNA and RNA-protein complexes RNA Editing RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism Serine-Arginine Splicing Factors - genetics Serine-Arginine Splicing Factors - metabolism |
| Title | Tissue-selective restriction of RNA editing of CaV1.3 by splicing factor SRSF9 |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/29733375 https://www.proquest.com/docview/2035707118 https://pubmed.ncbi.nlm.nih.gov/PMC6101491 |
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