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The Sam68 nuclear body is composed of two RNase-sensitive substructures joined by the adaptor HNRNPL
The mammalian cell nucleus contains membraneless suborganelles referred to as nuclear bodies (NBs). Some NBs are formed with an architectural RNA (arcRNA) as the structural core. Here, we searched for new NBs that are built on unidentified arcRNAs by screening for ribonuclease (RNase)-sensitive NBs...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4932371/ https://www.ncbi.nlm.nih.gov/pubmed/27377249 http://dx.doi.org/10.1083/jcb.201601024 |
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author | Mannen, Taro Yamashita, Seisuke Tomita, Kozo Goshima, Naoki Hirose, Tetsuro |
author_facet | Mannen, Taro Yamashita, Seisuke Tomita, Kozo Goshima, Naoki Hirose, Tetsuro |
author_sort | Mannen, Taro |
collection | PubMed |
description | The mammalian cell nucleus contains membraneless suborganelles referred to as nuclear bodies (NBs). Some NBs are formed with an architectural RNA (arcRNA) as the structural core. Here, we searched for new NBs that are built on unidentified arcRNAs by screening for ribonuclease (RNase)-sensitive NBs using 32,651 fluorescently tagged human cDNA clones. We identified 32 tagged proteins that required RNA for their localization in distinct nuclear foci. Among them, seven RNA-binding proteins commonly localized in the Sam68 nuclear body (SNB), which was disrupted by RNase treatment. Knockdown of each SNB protein revealed that SNBs are composed of two distinct RNase-sensitive substructures. One substructure is present as a distinct NB, termed the DBC1 body, in certain conditions, and the more dynamic substructure including Sam68 joins to form the intact SNB. HNRNPL acts as the adaptor to combine the two substructures and form the intact SNB through the interaction of two sets of RNA recognition motifs with the putative arcRNAs in the respective substructures. |
format | Online Article Text |
id | pubmed-4932371 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-49323712017-01-04 The Sam68 nuclear body is composed of two RNase-sensitive substructures joined by the adaptor HNRNPL Mannen, Taro Yamashita, Seisuke Tomita, Kozo Goshima, Naoki Hirose, Tetsuro J Cell Biol Research Articles The mammalian cell nucleus contains membraneless suborganelles referred to as nuclear bodies (NBs). Some NBs are formed with an architectural RNA (arcRNA) as the structural core. Here, we searched for new NBs that are built on unidentified arcRNAs by screening for ribonuclease (RNase)-sensitive NBs using 32,651 fluorescently tagged human cDNA clones. We identified 32 tagged proteins that required RNA for their localization in distinct nuclear foci. Among them, seven RNA-binding proteins commonly localized in the Sam68 nuclear body (SNB), which was disrupted by RNase treatment. Knockdown of each SNB protein revealed that SNBs are composed of two distinct RNase-sensitive substructures. One substructure is present as a distinct NB, termed the DBC1 body, in certain conditions, and the more dynamic substructure including Sam68 joins to form the intact SNB. HNRNPL acts as the adaptor to combine the two substructures and form the intact SNB through the interaction of two sets of RNA recognition motifs with the putative arcRNAs in the respective substructures. The Rockefeller University Press 2016-07-04 /pmc/articles/PMC4932371/ /pubmed/27377249 http://dx.doi.org/10.1083/jcb.201601024 Text en © 2016 Mannen et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Mannen, Taro Yamashita, Seisuke Tomita, Kozo Goshima, Naoki Hirose, Tetsuro The Sam68 nuclear body is composed of two RNase-sensitive substructures joined by the adaptor HNRNPL |
title | The Sam68 nuclear body is composed of two RNase-sensitive substructures joined by the adaptor HNRNPL |
title_full | The Sam68 nuclear body is composed of two RNase-sensitive substructures joined by the adaptor HNRNPL |
title_fullStr | The Sam68 nuclear body is composed of two RNase-sensitive substructures joined by the adaptor HNRNPL |
title_full_unstemmed | The Sam68 nuclear body is composed of two RNase-sensitive substructures joined by the adaptor HNRNPL |
title_short | The Sam68 nuclear body is composed of two RNase-sensitive substructures joined by the adaptor HNRNPL |
title_sort | sam68 nuclear body is composed of two rnase-sensitive substructures joined by the adaptor hnrnpl |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4932371/ https://www.ncbi.nlm.nih.gov/pubmed/27377249 http://dx.doi.org/10.1083/jcb.201601024 |
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