ADAR2 is a double-stranded-RNA-specific adenosine deaminase involved in the editing of mammalian RNAs by the site-selective conversion of adenosine to inosine. Previous studies from our laboratory have demonstrated that ADAR2 can modify its own pre-mRNA to create a proximal 3' splice site containing a noncanonical adenosine-inosine dinucleotide. Alternative splicing to this proximal acceptor adds 47 nucleotides to the mature ADAR2 transcript, thereby resulting in the loss of functional ADAR2 protein expression due to premature translation termination in an alternate reading frame. To examine whether the editing of ADAR2 transcripts represents a negative autoregulatory strategy to modulate ADAR2 protein expression, we have generated genetically modified mice in which the ability of ADAR2 to edit its own pre-mRNA has been selectively ablated by deletion of a critical sequence (editing site complementary sequence [ECS]) required for adenosine-to-inosine conversion. Here we demonstrate that ADAR2 autoediting and subsequent alternative splicing are abolished in homozygous deltaECS mice and that ADAR2 protein expression is increased in numerous tissues compared to wild-type animals. The observed increases in ADAR2 protein expression correlate with the extent of ADAR2 autoediting observed with wild-type tissues and correspond to increases in the editing of ADAR2 substrates, indicating that ADAR2 autoediting is a key regulator of ADAR2 protein expression and activity in vivo.
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http://dx.doi.org/10.1128/MCB.26.2.480-488.2006 | DOI Listing |
Cell Mol Biol Lett
January 2025
Key Laboratory of Neuro-Oncology in Liaoning Province, Shenyang, 110004, China.
Background: Glioblastoma multiforme (GBM) is a highly aggressive brain tumor, characterized by its poor prognosis. Glycolipid metabolism is strongly associated with GBM development and malignant behavior. However, the precise functions of snoRNAs and ADARs in glycolipid metabolism within GBM cells remain elusive.
View Article and Find Full Text PDFCytojournal
November 2024
Department of Neurosurgery, Guangzhou Red Cross Hospital, Jinan University, Guangzhou, China.
Objective: Potassium voltage-gated channel sub-family A member 1 (Kv1.1), as a shaker homolog potassium channel, displays a special mechanism for posttranscriptional regulation called RNA editing. Adenosine deaminase acting on RNA 2 (ADAR2) can cause abnormal editing or loss of normal editing, which results in cell damage and related diseases.
View Article and Find Full Text PDFRNA Biol
January 2024
School of Pharmacy, Shanghai University of Traditional Chinese Medicine, Shanghai, China.
The process of adenosine deaminase (ADAR)-catalyzed double-stranded RNA (dsRNA) Adenosine-to-Inosine (A-to-I) editing is essential for the correction of pathogenic mutagenesis, as well as the regulation of gene expression and protein function in mammals. The significance of dsRNA A-to-I editing in disease development and occurrence is explored using inferential statistics and cluster analyses to investigate the enzymes involved in dsRNA editing that can catalyze editing sites across multiple biomarkers. This editing process, which occurs in coding or non-coding regions, has the potential to activate abnormal signalling pathways that contributes to disease pathogenesis.
View Article and Find Full Text PDFNat Biotechnol
October 2024
School of Chemistry, Chemical Engineering and Biotechnology, Nanyang Technological University, Singapore, Singapore.
Biochemistry (Mosc)
August 2024
Pirogov Russian National Research Medical University, Moscow, 117997, Russia.
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