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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...

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Autores principales: Castle, Christopher D., Cassimere, Erica K., Denicourt, Catherine
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2012
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.
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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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