期刊
CELL
卷 153, 期 3, 页码 575-589出版社
CELL PRESS
DOI: 10.1016/j.cell.2013.03.024
关键词
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资金
- National Institutes of Health [GM040536, HL070045, HL099342]
- Ellison Medical Foundation [AG-55-2281-09]
- Commonwealth Universal Research Enhancement Program, Pennsylvania Department of Health
- University of Pennsylvania, Vagelos scholarship
- Japan Society for the Promotion of Science (JSPS) [2010-22]
- National Cancer Institute [P30 CA010815]
- Grants-in-Aid for Scientific Research [23590443] Funding Source: KAKEN
Adenosine deaminases acting on RNA (ADARs) are involved in RNA editing that converts adenosine residues to inosine specifically in double-stranded RNAs. In this study, we investigated the interaction of the RNA editing mechanism with the RNA interference (RNAi) machinery and found that ADAR1 forms a complex with Dicer through direct protein-protein interaction. Most importantly, ADAR1 increases the maximum rate (V-max) of pre-microRNA (miRNA) cleavage by Dicer and facilitates loading of miRNA onto RNA-induced silencing complexes, identifying a new role of ADAR1 in miRNA processing and RNAi mechanisms. ADAR1 differentiates its functions in RNA editing and RNAi by the formation of either ADAR1/ADAR1 homodimer or Dicer/ADAR1 heterodimer complexes, respectively. As expected, the expression of miRNAs is globally inhibited in ADAR1(-/-) mouse embryos, which, in turn, alters the expression of their target genes and might contribute to their embryonic lethal phenotype.
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