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Myo10 tail is crucial for promoting long filopodia.
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- Additional Information
- Source:
Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
- Publication Information:
Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
- Subject Terms:
- Abstract:
Filopodia are slender cellular protrusions containing parallel actin bundles involved in environmental sensing and signaling, cell adhesion and migration, and growth cone guidance and extension. Myosin 10 (Myo10), an unconventional actin-based motor protein, was reported to induce filopodial initiation with its motor domain. However, the roles of the multifunctional tail domain of Myo10 in filopodial formation and elongation remain elusive. Herein, we generated several constructs of Myo10-full-length Myo10, Myo10 with a truncated tail (Myo10 HMM), and Myo10 containing four mutations to disrupt its coiled-coil domain (Myo10 CC mutant). We found that the truncation of the tail domain decreased filopodial formation and filopodial length, while four mutations in the coiled-coil domain disrupted the motion of Myo10 toward filopodial tips and the elongation of filopodia. Furthermore, we found that filopodia elongated through multiple elongation cycles, which was supported by the Myo10 tail. These findings suggest that Myo10 tail is crucial for promoting long filopodia.
Competing Interests: Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.
(Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.)
- Grant Information:
R01 DC009100 United States DC NIDCD NIH HHS
- Contributed Indexing:
Keywords: coiled coil; dimerization; filopodia; filopodial elongation; heavy meromyosin; myosin 10
- Accession Number:
0 (Actins)
EC 3.6.4.1 (Myosins)
0 (MYO10 protein, human)
- Publication Date:
Date Created: 20231203 Date Completed: 20240209 Latest Revision: 20240209
- Publication Date:
20240210
- Accession Number:
PMC10790087
- Accession Number:
10.1016/j.jbc.2023.105523
- Accession Number:
38043799
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