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LAS1L interacts with the mammalian Rix1 complex to regulate ribosome biogenesis
The coordination of RNA polymerase I transcription with pre-rRNA processing, preribosomal particle assembly, and nuclear export is a finely tuned process requiring the concerted actions of a number of accessory factors. However, the exact functions of some of these proteins and how they assemble in...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3279398/ https://www.ncbi.nlm.nih.gov/pubmed/22190735 http://dx.doi.org/10.1091/mbc.E11-06-0530 |
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author | Castle, Christopher D. Cassimere, Erica K. Denicourt, Catherine |
author_facet | Castle, Christopher D. Cassimere, Erica K. Denicourt, Catherine |
author_sort | Castle, Christopher D. |
collection | PubMed |
description | The coordination of RNA polymerase I transcription with pre-rRNA processing, preribosomal particle assembly, and nuclear export is a finely tuned process requiring the concerted actions of a number of accessory factors. However, the exact functions of some of these proteins and how they assemble in subcomplexes remain poorly defined. LAS1L was first described as a nucleolar protein required for maturation of the 60S preribosomal subunit. In this paper, we demonstrate that LAS1L interacts with PELP1, TEX10, and WDR18, the mammalian homologues of the budding yeast Rix1 complex, along with NOL9 and SENP3, to form a novel nucleolar complex that cofractionates with the 60S preribosomal subunit. Depletion of LAS1L-associated proteins results in a p53-dependent G1 arrest and leads to defects in processing of the pre-rRNA internal transcribed spacer 2 region. We further show that the nucleolar localization of this complex requires active RNA polymerase I transcription and the small ubiquitin-like modifier–specific protease SENP3. Taken together, our data identify a novel mammalian complex required for 60S ribosomal subunit synthesis, providing further insight into the intricate, yet poorly described, process of ribosome biogenesis in higher eukaryotes. |
format | Online Article Text |
id | pubmed-3279398 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-32793982012-04-30 LAS1L interacts with the mammalian Rix1 complex to regulate ribosome biogenesis Castle, Christopher D. Cassimere, Erica K. Denicourt, Catherine Mol Biol Cell Articles The coordination of RNA polymerase I transcription with pre-rRNA processing, preribosomal particle assembly, and nuclear export is a finely tuned process requiring the concerted actions of a number of accessory factors. However, the exact functions of some of these proteins and how they assemble in subcomplexes remain poorly defined. LAS1L was first described as a nucleolar protein required for maturation of the 60S preribosomal subunit. In this paper, we demonstrate that LAS1L interacts with PELP1, TEX10, and WDR18, the mammalian homologues of the budding yeast Rix1 complex, along with NOL9 and SENP3, to form a novel nucleolar complex that cofractionates with the 60S preribosomal subunit. Depletion of LAS1L-associated proteins results in a p53-dependent G1 arrest and leads to defects in processing of the pre-rRNA internal transcribed spacer 2 region. We further show that the nucleolar localization of this complex requires active RNA polymerase I transcription and the small ubiquitin-like modifier–specific protease SENP3. Taken together, our data identify a novel mammalian complex required for 60S ribosomal subunit synthesis, providing further insight into the intricate, yet poorly described, process of ribosome biogenesis in higher eukaryotes. The American Society for Cell Biology 2012-02-15 /pmc/articles/PMC3279398/ /pubmed/22190735 http://dx.doi.org/10.1091/mbc.E11-06-0530 Text en © 2012 Castle 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 Biology. |
spellingShingle | Articles Castle, Christopher D. Cassimere, Erica K. Denicourt, Catherine LAS1L interacts with the mammalian Rix1 complex to regulate ribosome biogenesis |
title | LAS1L interacts with the mammalian Rix1 complex to regulate ribosome biogenesis |
title_full | LAS1L interacts with the mammalian Rix1 complex to regulate ribosome biogenesis |
title_fullStr | LAS1L interacts with the mammalian Rix1 complex to regulate ribosome biogenesis |
title_full_unstemmed | LAS1L interacts with the mammalian Rix1 complex to regulate ribosome biogenesis |
title_short | LAS1L interacts with the mammalian Rix1 complex to regulate ribosome biogenesis |
title_sort | las1l interacts with the mammalian rix1 complex to regulate ribosome biogenesis |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3279398/ https://www.ncbi.nlm.nih.gov/pubmed/22190735 http://dx.doi.org/10.1091/mbc.E11-06-0530 |
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