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The ERC1 scaffold protein implicated in cell motility drives the assembly of a liquid phase
Several cellular processes depend on networks of proteins assembled at specific sites near the plasma membrane. Scaffold proteins assemble these networks by recruiting relevant molecules. The scaffold protein ERC1/ELKS and its partners promote cell migration and invasion, and assemble into dynamic n...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6753080/ https://www.ncbi.nlm.nih.gov/pubmed/31537859 http://dx.doi.org/10.1038/s41598-019-49630-y |
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author | Sala, Kristyna Corbetta, Agnese Minici, Claudia Tonoli, Diletta Murray, David H. Cammarota, Eugenia Ribolla, Lucrezia Ramella, Martina Fesce, Riccardo Mazza, Davide Degano, Massimo de Curtis, Ivan |
author_facet | Sala, Kristyna Corbetta, Agnese Minici, Claudia Tonoli, Diletta Murray, David H. Cammarota, Eugenia Ribolla, Lucrezia Ramella, Martina Fesce, Riccardo Mazza, Davide Degano, Massimo de Curtis, Ivan |
author_sort | Sala, Kristyna |
collection | PubMed |
description | Several cellular processes depend on networks of proteins assembled at specific sites near the plasma membrane. Scaffold proteins assemble these networks by recruiting relevant molecules. The scaffold protein ERC1/ELKS and its partners promote cell migration and invasion, and assemble into dynamic networks at the protruding edge of cells. Here by electron microscopy and single molecule analysis we identify ERC1 as an extended flexible dimer. We found that ERC1 scaffolds form cytoplasmic condensates with a behavior that is consistent with liquid phases that are modulated by a predicted disordered region of ERC1. These condensates specifically host partners of a network relevant to cell motility, including liprin-α1, which was unnecessary for the formation of condensates, but influenced their dynamic behavior. Phase separation at specific sites of the cell periphery may represent an elegant mechanism to control the assembly and turnover of dynamic scaffolds needed for the spatial localization and processing of molecules. |
format | Online Article Text |
id | pubmed-6753080 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-67530802019-10-01 The ERC1 scaffold protein implicated in cell motility drives the assembly of a liquid phase Sala, Kristyna Corbetta, Agnese Minici, Claudia Tonoli, Diletta Murray, David H. Cammarota, Eugenia Ribolla, Lucrezia Ramella, Martina Fesce, Riccardo Mazza, Davide Degano, Massimo de Curtis, Ivan Sci Rep Article Several cellular processes depend on networks of proteins assembled at specific sites near the plasma membrane. Scaffold proteins assemble these networks by recruiting relevant molecules. The scaffold protein ERC1/ELKS and its partners promote cell migration and invasion, and assemble into dynamic networks at the protruding edge of cells. Here by electron microscopy and single molecule analysis we identify ERC1 as an extended flexible dimer. We found that ERC1 scaffolds form cytoplasmic condensates with a behavior that is consistent with liquid phases that are modulated by a predicted disordered region of ERC1. These condensates specifically host partners of a network relevant to cell motility, including liprin-α1, which was unnecessary for the formation of condensates, but influenced their dynamic behavior. Phase separation at specific sites of the cell periphery may represent an elegant mechanism to control the assembly and turnover of dynamic scaffolds needed for the spatial localization and processing of molecules. Nature Publishing Group UK 2019-09-19 /pmc/articles/PMC6753080/ /pubmed/31537859 http://dx.doi.org/10.1038/s41598-019-49630-y Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Sala, Kristyna Corbetta, Agnese Minici, Claudia Tonoli, Diletta Murray, David H. Cammarota, Eugenia Ribolla, Lucrezia Ramella, Martina Fesce, Riccardo Mazza, Davide Degano, Massimo de Curtis, Ivan The ERC1 scaffold protein implicated in cell motility drives the assembly of a liquid phase |
title | The ERC1 scaffold protein implicated in cell motility drives the assembly of a liquid phase |
title_full | The ERC1 scaffold protein implicated in cell motility drives the assembly of a liquid phase |
title_fullStr | The ERC1 scaffold protein implicated in cell motility drives the assembly of a liquid phase |
title_full_unstemmed | The ERC1 scaffold protein implicated in cell motility drives the assembly of a liquid phase |
title_short | The ERC1 scaffold protein implicated in cell motility drives the assembly of a liquid phase |
title_sort | erc1 scaffold protein implicated in cell motility drives the assembly of a liquid phase |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6753080/ https://www.ncbi.nlm.nih.gov/pubmed/31537859 http://dx.doi.org/10.1038/s41598-019-49630-y |
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