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...

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Main Authors: 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
Format: Article
Language:English
Published: Nature Portfolio 2019-08-01
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.
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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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