Myo10 tail is crucial for promoting long filopodia

J Biol Chem. 2024 Jan;300(1):105523. doi: 10.1016/j.jbc.2023.105523. Epub 2023 Dec 2.

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.

Keywords: coiled coil; dimerization; filopodia; filopodial elongation; heavy meromyosin; myosin 10.

MeSH terms

  • Actins / metabolism
  • Animals
  • COS Cells
  • Cell Adhesion
  • Chlorocebus aethiops
  • Humans
  • Myosins* / chemistry
  • Myosins* / genetics
  • Myosins* / metabolism
  • Protein Domains
  • Pseudopodia* / genetics
  • Pseudopodia* / metabolism

Substances

  • Actins
  • Myosins
  • MYO10 protein, human