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The m(6)A-methylase complex recruits TREX and regulates mRNA export
N(6)-methyladenosine (m(6)A) 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 comple...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6138711/ https://www.ncbi.nlm.nih.gov/pubmed/30218090 http://dx.doi.org/10.1038/s41598-018-32310-8 |
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author | Lesbirel, Simon Viphakone, Nicolas Parker, Matthew Parker, Jacob Heath, Catherine Sudbery, Ian Wilson, Stuart A. |
author_facet | Lesbirel, Simon Viphakone, Nicolas Parker, Matthew Parker, Jacob Heath, Catherine Sudbery, Ian Wilson, Stuart A. |
author_sort | Lesbirel, Simon |
collection | PubMed |
description | N(6)-methyladenosine (m(6)A) 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(6)A methylase complex. We show that the m(6)A complex recruits TREX to m(6)A modified mRNAs and this process is essential for their efficient export. TREX also stimulates recruitment of the m(6)A reader protein YTHDC1 to the mRNA and the m(6)A complex influences the interaction of TREX with YTHDC1. Together our studies reveal a key role for TREX in the export of m(6)A modified mRNAs. |
format | Online Article Text |
id | pubmed-6138711 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-61387112018-09-15 The m(6)A-methylase complex recruits TREX and regulates mRNA export Lesbirel, Simon Viphakone, Nicolas Parker, Matthew Parker, Jacob Heath, Catherine Sudbery, Ian Wilson, Stuart A. Sci Rep Article N(6)-methyladenosine (m(6)A) 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(6)A methylase complex. We show that the m(6)A complex recruits TREX to m(6)A modified mRNAs and this process is essential for their efficient export. TREX also stimulates recruitment of the m(6)A reader protein YTHDC1 to the mRNA and the m(6)A complex influences the interaction of TREX with YTHDC1. Together our studies reveal a key role for TREX in the export of m(6)A modified mRNAs. Nature Publishing Group UK 2018-09-14 /pmc/articles/PMC6138711/ /pubmed/30218090 http://dx.doi.org/10.1038/s41598-018-32310-8 Text en © The Author(s) 2018 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/. |
spellingShingle | Article Lesbirel, Simon Viphakone, Nicolas Parker, Matthew Parker, Jacob Heath, Catherine Sudbery, Ian Wilson, Stuart A. The m(6)A-methylase complex recruits TREX and regulates mRNA export |
title | The m(6)A-methylase complex recruits TREX and regulates mRNA export |
title_full | The m(6)A-methylase complex recruits TREX and regulates mRNA export |
title_fullStr | The m(6)A-methylase complex recruits TREX and regulates mRNA export |
title_full_unstemmed | The m(6)A-methylase complex recruits TREX and regulates mRNA export |
title_short | The m(6)A-methylase complex recruits TREX and regulates mRNA export |
title_sort | m(6)a-methylase complex recruits trex and regulates mrna export |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6138711/ https://www.ncbi.nlm.nih.gov/pubmed/30218090 http://dx.doi.org/10.1038/s41598-018-32310-8 |
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