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CMTr cap-adjacent 2`-O-ribose mRNA methyltransferases are required for reward learning
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Haussmann, Irmgard U., Wu, Yanying, Nallasivan, Mohanakarthik P., Archer, Nathan, Bodi, Zsuzsanna, Hebenstreit, Daniel, Waddell, Scott, Fray, Rupert and Soller, Matthias (2022) CMTr cap-adjacent 2`-O-ribose mRNA methyltransferases are required for reward learning. Nature Communications, 13 . 1209. doi:10.1038/s41467-022-28549-5
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WRAP-CMTr-cap-adjacent-2`-O-ribose-mRNA-methyltransferases-required-reward-learning-Hebenstreit-2022.pdf - Accepted Version Embargoed item. Restricted access to Repository staff only - Requires a PDF viewer. Download (6Mb) |
Official URL: https://doi.org/10.1038/s41467-022-28549-5
Abstract
Cap-adjacent nucleotides of animal, protist and viral mRNAs can be O-methylated at the 2‘ position of the ribose (cOMe). The functions of cOMe in animals, however, remain largely unknown. Here we show that the two cap methyltransferases (CMTr1 and CMTr2) of Drosophila can methylate the ribose of the first nucleotide in mRNA. Double-mutant flies lack cOMe but are viable. Consistent with prominent neuronal expression, they have a reward learning defect that can be rescued by conditional expression in mushroom body neurons before training. Among CMTr targets are cell adhesion and signaling molecules. Many are relevant for learning, and are also targets of Fragile X Mental Retardation Protein (FMRP). Like FMRP, cOMe is required for localization of untranslated mRNAs to synapses and enhances binding of the cap binding complex in the nucleus. Hence, our study reveals a mechanism to co-transcriptionally prime mRNAs by cOMe for localized protein synthesis at synapses.
| Item Type: | Journal Article | ||||||||||||||||||||||||||||||
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| Subjects: | Q Science > QH Natural history Q Science > QP Physiology |
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| Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||||||||||||||||||||||||||||
| Library of Congress Subject Headings (LCSH): | Messenger RNA, Gene expression, Nucleotides , Ribose | ||||||||||||||||||||||||||||||
| Journal or Publication Title: | Nature Communications | ||||||||||||||||||||||||||||||
| Publisher: | Nature Publishing Group | ||||||||||||||||||||||||||||||
| ISSN: | 2041-1723 | ||||||||||||||||||||||||||||||
| Official Date: | 8 March 2022 | ||||||||||||||||||||||||||||||
| Dates: |
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| Volume: | 13 | ||||||||||||||||||||||||||||||
| Article Number: | 1209 | ||||||||||||||||||||||||||||||
| DOI: | 10.1038/s41467-022-28549-5 | ||||||||||||||||||||||||||||||
| Status: | Peer Reviewed | ||||||||||||||||||||||||||||||
| Publication Status: | Published | ||||||||||||||||||||||||||||||
| Access rights to Published version: | Open Access | ||||||||||||||||||||||||||||||
| RIOXX Funder/Project Grant: |
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