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The RNA-binding protein Y14 inhibits mRNA decapping and modulates processing body formation
The exon-junction complex (EJC) deposited on a newly spliced mRNA plays an important role in subsequent mRNA metabolic events. Here we show that an EJC core heterodimer, Y14/Magoh, specifically associates with mRNA-degradation factors, including the mRNA-decapping complex and exoribonucleases, where...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3530774/ https://www.ncbi.nlm.nih.gov/pubmed/23115303 http://dx.doi.org/10.1091/mbc.E12-03-0217 |
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author | Chuang, Tzu-Wei Chang, Wei-Lun Lee, Kuo-Ming Tarn, Woan-Yuh |
author_facet | Chuang, Tzu-Wei Chang, Wei-Lun Lee, Kuo-Ming Tarn, Woan-Yuh |
author_sort | Chuang, Tzu-Wei |
collection | PubMed |
description | The exon-junction complex (EJC) deposited on a newly spliced mRNA plays an important role in subsequent mRNA metabolic events. Here we show that an EJC core heterodimer, Y14/Magoh, specifically associates with mRNA-degradation factors, including the mRNA-decapping complex and exoribonucleases, whereas another core factor, eIF4AIII/MLN51, does not. We also demonstrate that Y14 interacts directly with the decapping factor Dcp2 and the 5′ cap structure of mRNAs via different but overlapping domains and that Y14 inhibits the mRNA-decapping activity of Dcp2 in vitro. Accordingly, overexpression of Y14 prolongs the half-life of a reporter mRNA. Therefore Y14 may function independently of the EJC in preventing mRNA decapping and decay. Furthermore, we observe that depletion of Y14 disrupts the formation of processing bodies, whereas overexpression of a phosphomimetic Y14 considerably increases the number of processing bodies, perhaps by sequestering the mRNA-degradation factors. In conclusion, this report provides unprecedented evidence for a role of Y14 in regulating mRNA degradation and processing body formation and reinforces the influence of phosphorylation of Y14 on its activity in postsplicing mRNA metabolism. |
format | Online Article Text |
id | pubmed-3530774 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-35307742013-03-16 The RNA-binding protein Y14 inhibits mRNA decapping and modulates processing body formation Chuang, Tzu-Wei Chang, Wei-Lun Lee, Kuo-Ming Tarn, Woan-Yuh Mol Biol Cell Articles The exon-junction complex (EJC) deposited on a newly spliced mRNA plays an important role in subsequent mRNA metabolic events. Here we show that an EJC core heterodimer, Y14/Magoh, specifically associates with mRNA-degradation factors, including the mRNA-decapping complex and exoribonucleases, whereas another core factor, eIF4AIII/MLN51, does not. We also demonstrate that Y14 interacts directly with the decapping factor Dcp2 and the 5′ cap structure of mRNAs via different but overlapping domains and that Y14 inhibits the mRNA-decapping activity of Dcp2 in vitro. Accordingly, overexpression of Y14 prolongs the half-life of a reporter mRNA. Therefore Y14 may function independently of the EJC in preventing mRNA decapping and decay. Furthermore, we observe that depletion of Y14 disrupts the formation of processing bodies, whereas overexpression of a phosphomimetic Y14 considerably increases the number of processing bodies, perhaps by sequestering the mRNA-degradation factors. In conclusion, this report provides unprecedented evidence for a role of Y14 in regulating mRNA degradation and processing body formation and reinforces the influence of phosphorylation of Y14 on its activity in postsplicing mRNA metabolism. The American Society for Cell Biology 2013-01-01 /pmc/articles/PMC3530774/ /pubmed/23115303 http://dx.doi.org/10.1091/mbc.E12-03-0217 Text en © 2013 Chuang et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell BD; are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Chuang, Tzu-Wei Chang, Wei-Lun Lee, Kuo-Ming Tarn, Woan-Yuh The RNA-binding protein Y14 inhibits mRNA decapping and modulates processing body formation |
title | The RNA-binding protein Y14 inhibits mRNA decapping and modulates processing body formation |
title_full | The RNA-binding protein Y14 inhibits mRNA decapping and modulates processing body formation |
title_fullStr | The RNA-binding protein Y14 inhibits mRNA decapping and modulates processing body formation |
title_full_unstemmed | The RNA-binding protein Y14 inhibits mRNA decapping and modulates processing body formation |
title_short | The RNA-binding protein Y14 inhibits mRNA decapping and modulates processing body formation |
title_sort | rna-binding protein y14 inhibits mrna decapping and modulates processing body formation |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3530774/ https://www.ncbi.nlm.nih.gov/pubmed/23115303 http://dx.doi.org/10.1091/mbc.E12-03-0217 |
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