For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
4
views
14
references
 Top references
cited by
58
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      255
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      The m 6A-methylase complex recruits TREX and regulates mRNA export

      research-article

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          N 6-methyladenosine (m 6A) is the most abundant internal modification of eukaryotic mRNA. This modification has previously been shown to alter the export kinetics for mRNAs though the molecular details surrounding this phenomenon remain poorly understood. Recruitment of the TREX mRNA export complex to mRNA is driven by transcription, 5′ capping and pre-mRNA splicing. Here we identify a fourth mechanism in human cells driving the association of TREX with mRNA involving the m 6A methylase complex. We show that the m 6A complex recruits TREX to m 6A modified mRNAs and this process is essential for their efficient export. TREX also stimulates recruitment of the m 6A reader protein YTHDC1 to the mRNA and the m 6A complex influences the interaction of TREX with YTHDC1. Together our studies reveal a key role for TREX in the export of m 6A modified mRNAs.

          Related collections

          Most cited references14

          • Record: found
          • Abstract: found
          • Article: found
          Is Open Access

          featureCounts: An efficient general-purpose program for assigning sequence reads to genomic features

          , , (2013)
          Next-generation sequencing technologies generate millions of short sequence reads, which are usually aligned to a reference genome. In many applications, the key information required for downstream analysis is the number of reads mapping to each genomic feature, for example to each exon or each gene. The process of counting reads is called read summarization. Read summarization is required for a great variety of genomic analyses but has so far received relatively little attention in the literature. We present featureCounts, a read summarization program suitable for counting reads generated from either RNA or genomic DNA sequencing experiments. featureCounts implements highly efficient chromosome hashing and feature blocking techniques. It is considerably faster than existing methods (by an order of magnitude for gene-level summarization) and requires far less computer memory. It works with either single or paired-end reads and provides a wide range of options appropriate for different sequencing applications. featureCounts is available under GNU General Public License as part of the Subread (http://subread.sourceforge.net) or Rsubread (http://www.bioconductor.org) software packages.
          Article 0 comments Cited 770 times – based on 0 reviews
          Preprint
               Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: found
            Is Open Access

            Zc3h13/Flacc is required for adenosine methylation by bridging the mRNA-binding factor Rbm15/Spenito to the m 6A machinery component Wtap/Fl(2)d

            Philip Knuckles, Tina Lence, Irmgard Haussmann … (2018)
            In this study, Knuckles et al. identified Flacc/Zc3h13 as a novel interactor of m 6 A methyltransferase complex components in Drosophila and mice. They show that Flacc promotes the recruitment of the methyltransferase to mRNA by bridging Fl(2)d to the mRNA-binding factor Nito, providing novel insights into the conservation and regulation of the m 6 A machinery. N 6 -methyladenosine (m 6 A) is the most abundant mRNA modification in eukaryotes, playing crucial roles in multiple biological processes. m 6 A is catalyzed by the activity of methyltransferase-like 3 (Mettl3), which depends on additional proteins whose precise functions remain poorly understood. Here we identified Zc3h13 (zinc finger CCCH domain-containing protein 13)/Flacc [Fl(2)d-associated complex component] as a novel interactor of m 6 A methyltransferase complex components in Drosophila and mice. Like other components of this complex, Flacc controls m 6 A levels and is involved in sex determination in Drosophila . We demonstrate that Flacc promotes m 6 A deposition by bridging Fl(2)d to the mRNA-binding factor Nito. Altogether, our work advances the molecular understanding of conservation and regulation of the m 6 A machinery.
            Article 0 comments Cited 261 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Identification of Wilms' tumor 1-associating protein complex and its role in alternative splicing and the cell cycle.

              Keiko Horiuchi, Takeshi Kawamura, Hiroko Iwanari … (2013)
              Wilms' tumor 1-associating protein (WTAP) is a putative splicing regulator that is thought to be required for cell cycle progression through the stabilization of cyclin A2 mRNA and mammalian early embryo development. To further understand how WTAP acts in the context of the cellular machinery, we identified its interacting proteins in human umbilical vein endothelial cells and HeLa cells using shotgun proteomics. Here we show that WTAP forms a novel protein complex including Hakai, Virilizer homolog, KIAA0853, RBM15, the arginine/serine-rich domain-containing proteins BCLAF1 and THRAP3, and certain general splicing regulators, most of which have reported roles in post-transcriptional regulation. The depletion of these respective components of the complex resulted in reduced cell proliferation along with G2/M accumulation. Double knockdown of the serine/arginine-rich (SR)-like proteins BCLAF1 and THRAP3 by siRNA resulted in a decrease in the nuclear speckle localization of WTAP, whereas the nuclear speckles were intact. Furthermore, we found that the WTAP complex regulates alternative splicing of the WTAP pre-mRNA by promoting the production of a truncated isoform, leading to a change in WTAP protein expression. Collectively, these findings show that the WTAP complex is a novel component of the RNA processing machinery, implying an important role in both posttranscriptional control and cell cycle regulation.
              Article 0 comments Cited 159 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Contributors
                Stuart A. Wilson: stuart.wilson@sheffield.ac.uk
                Journal
                Journal ID (nlm-ta): Sci Rep
                Journal ID (iso-abbrev): Sci Rep
                Title: Scientific Reports
                Publisher: Nature Publishing Group UK (London )
                ISSN (Electronic): 2045-2322
                Publication date (Electronic): 14 September 2018
                Publication date PMC-release: 14 September 2018
                Publication date Collection: 2018
                Volume: 8
                Electronic Location Identifier: 13827
                Affiliations
                ISNI 0000 0004 1936 9262, GRID grid.11835.3e, Sheffield Institute For Nucleic Acids (SInFoNiA), Department of Molecular Biology and Biotechnology, , University of Sheffield, Firth Court Western Bank, ; Sheffield, S10 2TN UK
                Article
                Publisher ID: 32310
                DOI: 10.1038/s41598-018-32310-8
                PMC ID: 6138711
                PubMed ID: 30218090
                SO-VID: 7bea1195-f173-4e9a-a4dc-04e5288ad416
                Copyright © © The Author(s) 2018
                License:

                Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

                History
                Date received : 11 May 2018
                Date accepted : 4 September 2018
                Funding
                Funded by: FundRef https://doi.org/10.13039/501100000268, Biotechnology and Biological Sciences Research Council (BBSRC);
                Award ID: BB/N014839/1
                Award ID: BB/N005430/1
                Award Recipient :
                Categories
                Subject: Article
                Custom metadata
                issue-copyright-statement © The Author(s) 2018

                ScienceOpen disciplines: Uncategorized
                Data availability:
                ScienceOpen disciplines: Uncategorized

                Comments

                Comment on this article

                scite_

                Similar content255

                See all similar

                Cited by58

                See all cited by

                Most referenced authors1,045

                See all reference authors