Identification of z-axis filopodia in growth cones using super-resolution microscopy

J Neurochem. 2024 Sep;168(9):2974-2988. doi: 10.1111/jnc.16162. Epub 2024 Jul 1.

Abstract

A growth cone is a highly motile tip of an extending axon that is crucial for neural network formation. Three-dimensional-structured illumination microscopy, a type of super-resolution light microscopy with a resolution that overcomes the optical diffraction limitation (ca. 200 nm) of conventional light microscopy, is well suited for studying the molecular dynamics of intracellular events. Using this technique, we discovered a novel type of filopodia distributed along the z-axis ("z-filopodia") within the growth cone. Z-filopodia were typically oriented in the direction of axon growth, not attached to the substratum, protruded spontaneously without microtubule invasion, and had a lifetime that was considerably shorter than that of conventional filopodia. Z-filopodia formation and dynamics were regulated by actin-regulatory proteins, such as vasodilator-stimulated phosphoprotein, fascin, and cofilin. Chromophore-assisted laser inactivation of cofilin induced the rapid turnover of z-filopodia. An axon guidance receptor, neuropilin-1, was concentrated in z-filopodia and was transported together with them, whereas its ligand, semaphorin-3A, was selectively bound to them. Membrane domains associated with z-filopodia were also specialized and resembled those of lipid rafts, and their behaviors were closely related to those of neuropilin-1. The results suggest that z-filopodia have unique turnover properties, and unlike xy-filopodia, do not function as force-generating structures for axon extension.

Keywords: actin cytoskeleton; cofilin; growth cone; neuropilin‐1; structured illumination microscopy (SIM); super‐resolution microscopy.

MeSH terms

  • Actin Depolymerizing Factors / metabolism
  • Animals
  • Carrier Proteins / metabolism
  • Cell Adhesion Molecules
  • Cells, Cultured
  • Chick Embryo
  • Growth Cones* / metabolism
  • Microfilament Proteins / metabolism
  • Microscopy / methods
  • Neuropilin-1 / metabolism
  • Phosphoproteins / metabolism
  • Pseudopodia* / metabolism
  • Semaphorin-3A / metabolism
  • Vasodilator-Stimulated Phosphoprotein

Substances

  • Microfilament Proteins
  • Neuropilin-1
  • Vasodilator-Stimulated Phosphoprotein
  • Actin Depolymerizing Factors
  • Semaphorin-3A
  • Carrier Proteins
  • fascin
  • Phosphoproteins
  • Cell Adhesion Molecules