The plakin Short Stop and the RhoA GTPase are required for E-cadherin-dependent apical surface remodeling during tracheal tube fusion

Development. 2002 Mar;129(6):1509-20.

Abstract

Cells in vascular and other tubular networks require apical polarity in order to contact each other properly and to form lumen. As tracheal branches join together in Drosophila melanogaster embryos, specialized cells at the junction form a new E-cadherin-based contact and assemble an associated track of F-actin and the plakin Short Stop (shot). In these fusion cells, the apical surface determinant Discs Lost (Dlt) is subsequently deposited and new lumen forms along the track. In shot mutant embryos, the fusion cells fail to remodel the initial E-cadherin contact, to make an associated F-actin structure and to form lumenal connections between tracheal branches. Shot binding to F-actin and microtubules is required to rescue these defects. This finding has led us to investigate whether other regulators of the F-actin cytoskeleton similarly affect apical cell surface remodeling and lumen formation. Expression of constitutively active RhoA in all tracheal cells mimics the shot phenotype and affects Shot localization in fusion cells. The dominant negative RhoA phenotype suggests that RhoA controls apical surface formation throughout the trachea. We therefore propose that in fusion cells, Shot may function downstream of RhoA to form E-cadherin-associated cytoskeletal structures that are necessary for apical determinant localization.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cadherins / physiology*
  • Cell Differentiation
  • Cell Polarity / physiology
  • Cytoskeleton / physiology
  • Drosophila Proteins / physiology*
  • Drosophila melanogaster / embryology*
  • Drosophila melanogaster / physiology
  • Microfilament Proteins / physiology*
  • Morphogenesis
  • Mutation
  • Trachea / embryology*
  • Trachea / physiology
  • rhoA GTP-Binding Protein / physiology*

Substances

  • Cadherins
  • Drosophila Proteins
  • Microfilament Proteins
  • shot protein, Drosophila
  • rhoA GTP-Binding Protein