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• W2795649819 endingPage "1005" @default.
• W2795649819 startingPage "986" @default.
• W2795649819 abstract "Methylations at position N6 of internal adenosines (m6As) are the most abundant and widespread mRNA modifications. These modifications play crucial roles in reproduction, growth, and development by controlling gene expression patterns at the posttranscriptional level. Their function is decoded by readers that share the YTH domain, which forms a hydrophobic pocket that directly accommodates the m6A residues. While the physiological and molecular functions of YTH readers have been extensively studied in animals, little is known about plant readers, even though m6As are crucial for plant survival and development. Viridiplantae contains high numbers of YTH domain proteins. Here, we performed comprehensive evolutionary analysis of YTH domain proteins and demonstrated that they are highly likely to be actual readers with redundant as well as specific functions. We also show that the ECT2 protein from Arabidopsis thaliana binds to m6A-containing RNAs in vivo and that this property relies on the m6A binding pocket carried by its YTH domain. ECT2 is cytoplasmic and relocates to stress granules upon heat exposure, suggesting that it controls mRNA fate in the cytosol. Finally, we demonstrate that ECT2 acts to decode the m6A signal in the trichome and is required for their normal branching through controlling their ploidy levels." @default.
• W2795649819 created "2018-04-13" @default.
• W2795649819 creator A5008492856 @default.
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• W2795649819 date "2018-04-04" @default.
• W2795649819 modified "2023-10-11" @default.
• W2795649819 title "The YTH Domain Protein ECT2 Is an m⁶A Reader Required for Normal Trichome Branching in Arabidopsis" @default.
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• W2795649819 doi "https://doi.org/10.1105/tpc.17.00854" @default.
• W2795649819 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6002185" @default.
• W2795649819 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29618631" @default.
• W2795649819 hasPublicationYear "2018" @default.
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