Myosin X is recruited to nascent focal adhesions at the leading edge and induces multi-cycle filopodial elongation
Abstract Filopodia protrude from the leading edge of cells and play important roles in cell motility. Here we report the mechanism of myosin X (encoded by Myo10)-induced multi-cycle filopodia extension. We found that actin, Arp2/3, vinculin and integrin-β first accumulated at the cell’s leading edge...
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2017
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oai:doaj.org-article:1d9aaba67a494c1db325ab4a0b2f64672021-12-02T15:05:38ZMyosin X is recruited to nascent focal adhesions at the leading edge and induces multi-cycle filopodial elongation10.1038/s41598-017-06147-62045-2322https://doaj.org/article/1d9aaba67a494c1db325ab4a0b2f64672017-10-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-06147-6https://doaj.org/toc/2045-2322Abstract Filopodia protrude from the leading edge of cells and play important roles in cell motility. Here we report the mechanism of myosin X (encoded by Myo10)-induced multi-cycle filopodia extension. We found that actin, Arp2/3, vinculin and integrin-β first accumulated at the cell’s leading edge. Myosin X was then gathered at these sites, gradually clustered by lateral movement, and subsequently initiated filopodia formation. During filopodia extension, we found the translocation of Arp2/3 and integrin-β along filopodia. Arp2/3 and integrin-β then became localized at the tip of filopodia, from where myosin X initiated the second extension of filopodia with a change in extension direction, thus producing long filopodia. Elimination of integrin-β, Arp2/3 and vinculin by siRNA significantly attenuated the myosin-X-induced long filopodia formation. We propose the following mechanism. Myosin X accumulates at nascent focal adhesions at the cell’s leading edge, where myosin X promotes actin convergence to create the base of filopodia. Then myosin X moves to the filopodia tip and attracts integrin-β and Arp2/3 for further actin nucleation. The tip-located myosin X then initiates the second cycle of filopodia elongation to produce the long filopodia.Kangmin HeTsuyoshi SakaiYoshikazu TsukasakiTomonobu M. WatanabeMitsuo IkebeNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-12 (2017) |
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Medicine R Science Q Kangmin He Tsuyoshi Sakai Yoshikazu Tsukasaki Tomonobu M. Watanabe Mitsuo Ikebe Myosin X is recruited to nascent focal adhesions at the leading edge and induces multi-cycle filopodial elongation |
description |
Abstract Filopodia protrude from the leading edge of cells and play important roles in cell motility. Here we report the mechanism of myosin X (encoded by Myo10)-induced multi-cycle filopodia extension. We found that actin, Arp2/3, vinculin and integrin-β first accumulated at the cell’s leading edge. Myosin X was then gathered at these sites, gradually clustered by lateral movement, and subsequently initiated filopodia formation. During filopodia extension, we found the translocation of Arp2/3 and integrin-β along filopodia. Arp2/3 and integrin-β then became localized at the tip of filopodia, from where myosin X initiated the second extension of filopodia with a change in extension direction, thus producing long filopodia. Elimination of integrin-β, Arp2/3 and vinculin by siRNA significantly attenuated the myosin-X-induced long filopodia formation. We propose the following mechanism. Myosin X accumulates at nascent focal adhesions at the cell’s leading edge, where myosin X promotes actin convergence to create the base of filopodia. Then myosin X moves to the filopodia tip and attracts integrin-β and Arp2/3 for further actin nucleation. The tip-located myosin X then initiates the second cycle of filopodia elongation to produce the long filopodia. |
format |
article |
author |
Kangmin He Tsuyoshi Sakai Yoshikazu Tsukasaki Tomonobu M. Watanabe Mitsuo Ikebe |
author_facet |
Kangmin He Tsuyoshi Sakai Yoshikazu Tsukasaki Tomonobu M. Watanabe Mitsuo Ikebe |
author_sort |
Kangmin He |
title |
Myosin X is recruited to nascent focal adhesions at the leading edge and induces multi-cycle filopodial elongation |
title_short |
Myosin X is recruited to nascent focal adhesions at the leading edge and induces multi-cycle filopodial elongation |
title_full |
Myosin X is recruited to nascent focal adhesions at the leading edge and induces multi-cycle filopodial elongation |
title_fullStr |
Myosin X is recruited to nascent focal adhesions at the leading edge and induces multi-cycle filopodial elongation |
title_full_unstemmed |
Myosin X is recruited to nascent focal adhesions at the leading edge and induces multi-cycle filopodial elongation |
title_sort |
myosin x is recruited to nascent focal adhesions at the leading edge and induces multi-cycle filopodial elongation |
publisher |
Nature Portfolio |
publishDate |
2017 |
url |
https://doaj.org/article/1d9aaba67a494c1db325ab4a0b2f6467 |
work_keys_str_mv |
AT kangminhe myosinxisrecruitedtonascentfocaladhesionsattheleadingedgeandinducesmulticyclefilopodialelongation AT tsuyoshisakai myosinxisrecruitedtonascentfocaladhesionsattheleadingedgeandinducesmulticyclefilopodialelongation AT yoshikazutsukasaki myosinxisrecruitedtonascentfocaladhesionsattheleadingedgeandinducesmulticyclefilopodialelongation AT tomonobumwatanabe myosinxisrecruitedtonascentfocaladhesionsattheleadingedgeandinducesmulticyclefilopodialelongation AT mitsuoikebe myosinxisrecruitedtonascentfocaladhesionsattheleadingedgeandinducesmulticyclefilopodialelongation |
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1718388752550723584 |