Nuclear m(6)A Reader YTHDC1 Regulates mRNA Splicing.

Nuclear mA Reader YTHDC1 Regulates mRNA Splicing

YTHDC1 mediates nuclear export of N6-methyladenosine methylated mRNAs

N6-methyladenosine (m6A) is the most abundant internal modification of eukaryotic messenger RNA (mRNA) and plays critical roles in RNA biology. The function of this modification is mediated by m6A-selective 'reader' proteins of the YTH family, which incorporate m6A-modified mRNAs into pathways of RNA metabolism. Here, we show that the m6A-binding protein YTHDC1 mediates export of methylated mRN...

New Edges of RNA Adenosine Methylation Modifications

Recently an article published in Molecular Cell reveals the mechanism of a nuclear N-methyladenosine (mA) reader, the YTH domain-containing protein 1 (YTHDC1), in regulating pre-mRNA splicing [1]. Meanwhile, two additional articles published in Nature and Nature Chemical Biology report the first transcriptome-wide maps of N-methyladenosine (mA) at high resolution, suggesting a functional role f...

The interaction and colocalization of Sam68 with the splicing-associated factor YT521-B in nuclear dots is regulated by the Src family kinase p59(fyn).

Alternative pre-mRNA splicing patterns can change an extracellular stimulus, but the signaling pathways leading to these changes are still poorly characterized. Here, we describe a tyrosine-phosphorylated nuclear protein, YT521-B, and show that it interacts with the nuclear transcriptosomal component scaffold attachment factor B, and the 68-kDa Src substrate associated during mitosis, Sam68. No...

TITLE : C 3 G dynamically associates with Nuclear speckles and regulates mRNA splicing RUNNING HEAD : C 3 G regulates splicing AUTHORS : Dhruv