Fascin Regulates Nuclear Movement and Deformation in Migrating Cells

Fascin Regulates Nuclear Movement and Deformation in Migrating Cells

Fascin is an F-actin-bundling protein shown to stabilize filopodia and regulate adhesion dynamics in migrating cells, and its expression is correlated with poor prognosis and increased metastatic potential in a number of cancers. Here, we identified the nuclear envelope protein nesprin-2 as a bindin...

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Main Authors: Jayo, Asier, Malboubi, Majid, Antoku, Susumu, Chang, Wakam, Ortiz-Zapater, Elena, Groen, Christopher, Pfisterer, Karin, Tootle, Tina, Charras, Guillaume, Gundersen, Gregg G., Parsons, Maddy
Format: Online
Language:English
Published: Cell Press 2016
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4997957/
id pubmed-4997957
recordtype oai_dc
spelling pubmed-49979572016-09-01 Fascin Regulates Nuclear Movement and Deformation in Migrating Cells Jayo, Asier Malboubi, Majid Antoku, Susumu Chang, Wakam Ortiz-Zapater, Elena Groen, Christopher Pfisterer, Karin Tootle, Tina Charras, Guillaume Gundersen, Gregg G. Parsons, Maddy Article Fascin is an F-actin-bundling protein shown to stabilize filopodia and regulate adhesion dynamics in migrating cells, and its expression is correlated with poor prognosis and increased metastatic potential in a number of cancers. Here, we identified the nuclear envelope protein nesprin-2 as a binding partner for fascin in a range of cell types in vitro and in vivo. Nesprin-2 interacts with fascin through a direct, F-actin-independent interaction, and this binding is distinct and separable from a role for fascin within filopodia at the cell periphery. Moreover, disrupting the interaction between fascin and nesprin-2 C-terminal domain leads to specific defects in F-actin coupling to the nuclear envelope, nuclear movement, and the ability of cells to deform their nucleus to invade through confined spaces. Together, our results uncover a role for fascin that operates independently of filopodia assembly to promote efficient cell migration and invasion. Cell Press 2016-08-22 /pmc/articles/PMC4997957/ /pubmed/27554857 http://dx.doi.org/10.1016/j.devcel.2016.07.021 Text en © 2016 The Author(s) http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Jayo, Asier
Malboubi, Majid
Antoku, Susumu
Chang, Wakam
Ortiz-Zapater, Elena
Groen, Christopher
Pfisterer, Karin
Tootle, Tina
Charras, Guillaume
Gundersen, Gregg G.
Parsons, Maddy
spellingShingle Jayo, Asier
Malboubi, Majid
Antoku, Susumu
Chang, Wakam
Ortiz-Zapater, Elena
Groen, Christopher
Pfisterer, Karin
Tootle, Tina
Charras, Guillaume
Gundersen, Gregg G.
Parsons, Maddy
Fascin Regulates Nuclear Movement and Deformation in Migrating Cells
author_facet Jayo, Asier
Malboubi, Majid
Antoku, Susumu
Chang, Wakam
Ortiz-Zapater, Elena
Groen, Christopher
Pfisterer, Karin
Tootle, Tina
Charras, Guillaume
Gundersen, Gregg G.
Parsons, Maddy
author_sort Jayo, Asier
title Fascin Regulates Nuclear Movement and Deformation in Migrating Cells
title_short Fascin Regulates Nuclear Movement and Deformation in Migrating Cells
title_full Fascin Regulates Nuclear Movement and Deformation in Migrating Cells
title_fullStr Fascin Regulates Nuclear Movement and Deformation in Migrating Cells
title_full_unstemmed Fascin Regulates Nuclear Movement and Deformation in Migrating Cells
title_sort fascin regulates nuclear movement and deformation in migrating cells
description Fascin is an F-actin-bundling protein shown to stabilize filopodia and regulate adhesion dynamics in migrating cells, and its expression is correlated with poor prognosis and increased metastatic potential in a number of cancers. Here, we identified the nuclear envelope protein nesprin-2 as a binding partner for fascin in a range of cell types in vitro and in vivo. Nesprin-2 interacts with fascin through a direct, F-actin-independent interaction, and this binding is distinct and separable from a role for fascin within filopodia at the cell periphery. Moreover, disrupting the interaction between fascin and nesprin-2 C-terminal domain leads to specific defects in F-actin coupling to the nuclear envelope, nuclear movement, and the ability of cells to deform their nucleus to invade through confined spaces. Together, our results uncover a role for fascin that operates independently of filopodia assembly to promote efficient cell migration and invasion.
publisher Cell Press
publishDate 2016
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4997957/
_version_ 1613634958754054144

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