Myosin IIA and formin dependent mechanosensitivity of filopodia adhesion
Fiolopodia are involved in cell migration and their attachment to the ECM is mediated by integrin receptors. Here the authors show that myosin X induced filipodia adhesion to fibronectin requires activity of myosin IIA at the filopodium base and formin at the tip to support force transmission throug...
Main Authors: | , , , , , , , , , , , , |
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Format: | Article |
Language: | English |
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Nature Portfolio
2019-08-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-019-10964-w |
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author | N. O. Alieva A. K. Efremov S. Hu D. Oh Z. Chen M. Natarajan H. T. Ong A. Jégou G. Romet-Lemonne J. T. Groves M. P. Sheetz J. Yan A. D. Bershadsky |
author_facet | N. O. Alieva A. K. Efremov S. Hu D. Oh Z. Chen M. Natarajan H. T. Ong A. Jégou G. Romet-Lemonne J. T. Groves M. P. Sheetz J. Yan A. D. Bershadsky |
author_sort | N. O. Alieva |
collection | DOAJ |
description | Fiolopodia are involved in cell migration and their attachment to the ECM is mediated by integrin receptors. Here the authors show that myosin X induced filipodia adhesion to fibronectin requires activity of myosin IIA at the filopodium base and formin at the tip to support force transmission through the actin core. |
first_indexed | 2024-12-13T16:17:28Z |
format | Article |
id | doaj.art-239c9ca67f0f454d9d9ef6109dc7854c |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-13T16:17:28Z |
publishDate | 2019-08-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
spelling | doaj.art-239c9ca67f0f454d9d9ef6109dc7854c2022-12-21T23:38:48ZengNature PortfolioNature Communications2041-17232019-08-0110111410.1038/s41467-019-10964-wMyosin IIA and formin dependent mechanosensitivity of filopodia adhesionN. O. Alieva0A. K. Efremov1S. Hu2D. Oh3Z. Chen4M. Natarajan5H. T. Ong6A. Jégou7G. Romet-Lemonne8J. T. Groves9M. P. Sheetz10J. Yan11A. D. Bershadsky12Mechanobiology Institute, National University of Singapore, T-labMechanobiology Institute, National University of Singapore, T-labMechanobiology Institute, National University of Singapore, T-labMechanobiology Institute, National University of Singapore, T-labMechanobiology Institute, National University of Singapore, T-labMechanobiology Institute, National University of Singapore, T-labMechanobiology Institute, National University of Singapore, T-labInstitut Jacques Monod, CNRS, Université de ParisInstitut Jacques Monod, CNRS, Université de ParisMechanobiology Institute, National University of Singapore, T-labMechanobiology Institute, National University of Singapore, T-labMechanobiology Institute, National University of Singapore, T-labMechanobiology Institute, National University of Singapore, T-labFiolopodia are involved in cell migration and their attachment to the ECM is mediated by integrin receptors. Here the authors show that myosin X induced filipodia adhesion to fibronectin requires activity of myosin IIA at the filopodium base and formin at the tip to support force transmission through the actin core.https://doi.org/10.1038/s41467-019-10964-w |
spellingShingle | N. O. Alieva A. K. Efremov S. Hu D. Oh Z. Chen M. Natarajan H. T. Ong A. Jégou G. Romet-Lemonne J. T. Groves M. P. Sheetz J. Yan A. D. Bershadsky Myosin IIA and formin dependent mechanosensitivity of filopodia adhesion Nature Communications |
title | Myosin IIA and formin dependent mechanosensitivity of filopodia adhesion |
title_full | Myosin IIA and formin dependent mechanosensitivity of filopodia adhesion |
title_fullStr | Myosin IIA and formin dependent mechanosensitivity of filopodia adhesion |
title_full_unstemmed | Myosin IIA and formin dependent mechanosensitivity of filopodia adhesion |
title_short | Myosin IIA and formin dependent mechanosensitivity of filopodia adhesion |
title_sort | myosin iia and formin dependent mechanosensitivity of filopodia adhesion |
url | https://doi.org/10.1038/s41467-019-10964-w |
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