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The DEAD-Box RNA Helicase DDX3 Interacts with m(6)A RNA Demethylase ALKBH5

DDX3 is a member of the family of DEAD-box RNA helicases. DDX3 is a multifaceted helicase and plays essential roles in key biological processes such as cell cycle, stress response, apoptosis, and RNA metabolism. In this study, we found that DDX3 interacted with ALKBH5, an m(6)A RNA demethylase. The...

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Detalles Bibliográficos
Autores principales: Shah, Abdullah, Rashid, Farooq, Awan, Hassaan Mehboob, Hu, Shanshan, Wang, Xiaolin, Chen, Liang, Shan, Ge
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5733242/
https://www.ncbi.nlm.nih.gov/pubmed/29333169
http://dx.doi.org/10.1155/2017/8596135
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author Shah, Abdullah
Rashid, Farooq
Awan, Hassaan Mehboob
Hu, Shanshan
Wang, Xiaolin
Chen, Liang
Shan, Ge
author_facet Shah, Abdullah
Rashid, Farooq
Awan, Hassaan Mehboob
Hu, Shanshan
Wang, Xiaolin
Chen, Liang
Shan, Ge
author_sort Shah, Abdullah
collection PubMed
description DDX3 is a member of the family of DEAD-box RNA helicases. DDX3 is a multifaceted helicase and plays essential roles in key biological processes such as cell cycle, stress response, apoptosis, and RNA metabolism. In this study, we found that DDX3 interacted with ALKBH5, an m(6)A RNA demethylase. The ATP domain of DDX3 and DSBH domain of ALKBH5 were indispensable to their interaction with each other. Furthermore, DDX3 could modulate the demethylation of mRNAs. We also showed that DDX3 regulated the methylation status of microRNAs and there was an interaction between DDX3 and AGO2. The dynamics of m(6)A RNA modification is still a field demanding further investigation, and here, we add a link by showing that RNA demethylation can be regulated by proteins such as DDX3.
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spelling pubmed-57332422018-01-14 The DEAD-Box RNA Helicase DDX3 Interacts with m(6)A RNA Demethylase ALKBH5 Shah, Abdullah Rashid, Farooq Awan, Hassaan Mehboob Hu, Shanshan Wang, Xiaolin Chen, Liang Shan, Ge Stem Cells Int Research Article DDX3 is a member of the family of DEAD-box RNA helicases. DDX3 is a multifaceted helicase and plays essential roles in key biological processes such as cell cycle, stress response, apoptosis, and RNA metabolism. In this study, we found that DDX3 interacted with ALKBH5, an m(6)A RNA demethylase. The ATP domain of DDX3 and DSBH domain of ALKBH5 were indispensable to their interaction with each other. Furthermore, DDX3 could modulate the demethylation of mRNAs. We also showed that DDX3 regulated the methylation status of microRNAs and there was an interaction between DDX3 and AGO2. The dynamics of m(6)A RNA modification is still a field demanding further investigation, and here, we add a link by showing that RNA demethylation can be regulated by proteins such as DDX3. Hindawi 2017 2017-11-23 /pmc/articles/PMC5733242/ /pubmed/29333169 http://dx.doi.org/10.1155/2017/8596135 Text en Copyright © 2017 Abdullah Shah et al. http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Shah, Abdullah
Rashid, Farooq
Awan, Hassaan Mehboob
Hu, Shanshan
Wang, Xiaolin
Chen, Liang
Shan, Ge
The DEAD-Box RNA Helicase DDX3 Interacts with m(6)A RNA Demethylase ALKBH5
title The DEAD-Box RNA Helicase DDX3 Interacts with m(6)A RNA Demethylase ALKBH5
title_full The DEAD-Box RNA Helicase DDX3 Interacts with m(6)A RNA Demethylase ALKBH5
title_fullStr The DEAD-Box RNA Helicase DDX3 Interacts with m(6)A RNA Demethylase ALKBH5
title_full_unstemmed The DEAD-Box RNA Helicase DDX3 Interacts with m(6)A RNA Demethylase ALKBH5
title_short The DEAD-Box RNA Helicase DDX3 Interacts with m(6)A RNA Demethylase ALKBH5
title_sort dead-box rna helicase ddx3 interacts with m(6)a rna demethylase alkbh5
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5733242/
https://www.ncbi.nlm.nih.gov/pubmed/29333169
http://dx.doi.org/10.1155/2017/8596135
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