Anillin Regulates Neuronal Migration and Neurite Growth by Linking RhoG to the Actin Cytoskeleton

Curr Biol. 2015 May 4;25(9):1135-45. doi: 10.1016/j.cub.2015.02.072. Epub 2015 Apr 2.

Abstract

Neuronal migration and neurite growth are essential events in neural development, but it remains unclear how guidance cues are transduced through receptors to the actin cytoskeleton, which powers these processes. We report that a cytokinetic scaffold protein, Anillin, is redistributed to the leading edge of the C. elegans Q neuroblast during cell migration and neurite growth. To bypass the requirement for Anillin in cytokinesis, we used the somatic CRISPR-Cas9 technique to generate conditional mutations in Anillin. We demonstrate that Anillin regulates cell migration and growth cone extension by stabilizing the F-actin network at the leading edge. Our biochemical analysis shows that the actin-binding domain of Anillin is sufficient to stabilize F-actin by antagonizing the F-actin severing activity of Cofilin. We further uncover that the active form of RhoG/MIG-2 directly binds to Anillin and recruits it to the leading edge. Our results reveal a novel pathway in which Anillin transduces the RhoG signal to the actin cytoskeleton during neuronal migration and neurite growth.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actin Cytoskeleton / metabolism*
  • Actin Depolymerizing Factors / metabolism
  • Animals
  • CRISPR-Cas Systems
  • Caenorhabditis elegans
  • Caenorhabditis elegans Proteins / metabolism*
  • Cell Movement
  • Gene Knockout Techniques
  • Microfilament Proteins / metabolism*
  • Neurites / physiology*
  • rac GTP-Binding Proteins / metabolism*
  • rho GTP-Binding Proteins / metabolism

Substances

  • ANI-1 protein, C elegans
  • Actin Depolymerizing Factors
  • Caenorhabditis elegans Proteins
  • Microfilament Proteins
  • Mig-2 protein, C elegans
  • rac GTP-Binding Proteins
  • rho GTP-Binding Proteins