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Paraspeckles: Paragons of functional aggregation
Low-complexity proteins undergo phase separation in vitro, forming hydrogels or liquid droplets. Whether these form in vivo, and under what conditions, is still unclear. In this issue, Hennig et al. (2015. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201504117) show that formation of the paraspeckle,...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The Rockefeller University Press
2015
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4539984/ https://www.ncbi.nlm.nih.gov/pubmed/26283795 http://dx.doi.org/10.1083/jcb.201507052 |
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author | Courchaine, Edward Neugebauer, Karla M. |
author_facet | Courchaine, Edward Neugebauer, Karla M. |
author_sort | Courchaine, Edward |
collection | PubMed |
description | Low-complexity proteins undergo phase separation in vitro, forming hydrogels or liquid droplets. Whether these form in vivo, and under what conditions, is still unclear. In this issue, Hennig et al. (2015. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201504117) show that formation of the paraspeckle, a nuclear body that regulates gene expression, requires low-complexity prion-like domains (PLDs) within paraspeckle proteins. The same proteins were shown to form hydrogels, shedding light on the role of “functional aggregation” in nuclear substructure. |
format | Online Article Text |
id | pubmed-4539984 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-45399842016-02-17 Paraspeckles: Paragons of functional aggregation Courchaine, Edward Neugebauer, Karla M. J Cell Biol Reviews Low-complexity proteins undergo phase separation in vitro, forming hydrogels or liquid droplets. Whether these form in vivo, and under what conditions, is still unclear. In this issue, Hennig et al. (2015. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201504117) show that formation of the paraspeckle, a nuclear body that regulates gene expression, requires low-complexity prion-like domains (PLDs) within paraspeckle proteins. The same proteins were shown to form hydrogels, shedding light on the role of “functional aggregation” in nuclear substructure. The Rockefeller University Press 2015-08-17 /pmc/articles/PMC4539984/ /pubmed/26283795 http://dx.doi.org/10.1083/jcb.201507052 Text en © 2015 Neugebauer and Courchaine 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 | Reviews Courchaine, Edward Neugebauer, Karla M. Paraspeckles: Paragons of functional aggregation |
title | Paraspeckles: Paragons of functional aggregation |
title_full | Paraspeckles: Paragons of functional aggregation |
title_fullStr | Paraspeckles: Paragons of functional aggregation |
title_full_unstemmed | Paraspeckles: Paragons of functional aggregation |
title_short | Paraspeckles: Paragons of functional aggregation |
title_sort | paraspeckles: paragons of functional aggregation |
topic | Reviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4539984/ https://www.ncbi.nlm.nih.gov/pubmed/26283795 http://dx.doi.org/10.1083/jcb.201507052 |
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