Interplay of MPP5a with Rab11 synergistically builds epithelial apical polarity and zonula adherens

Development. 2020 Nov 19;147(22):dev184457. doi: 10.1242/dev.184457.

Abstract

Adherens junction remodeling regulated by apical polarity proteins constitutes a major driving force for tissue morphogenesis, although the precise mechanism remains inconclusive. Here, we report that, in zebrafish, the Crumbs complex component MPP5a interacts with small GTPase Rab11 in Golgi to transport cadherin and Crumbs components synergistically to the apical domain, thus establishing apical epithelial polarity and adherens junctions. In contrast, Par complex recruited by MPP5a is incapable of interacting with Rab11 but might assemble cytoskeleton to facilitate cadherin exocytosis. In accordance, dysfunction of MPP5a induces an invasive migration of epithelial cells. This adherens junction remodeling pattern is frequently observed in zebrafish lens epithelial cells and neuroepithelial cells. The data identify an unrecognized MPP5a-Rab11 complex and describe its essential role in guiding apical polarization and zonula adherens formation in epithelial cells.

Keywords: Adherens junctions remodeling; Apical polarity; MPP5a; Rab11; Zonula adherens.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adherens Junctions / genetics
  • Adherens Junctions / metabolism*
  • Animals
  • Cadherins / genetics
  • Cadherins / metabolism
  • Cell Movement / physiology*
  • Cell Polarity / physiology*
  • Epithelial Cells
  • Golgi Apparatus / genetics
  • Golgi Apparatus / metabolism
  • Guanylate Cyclase / genetics
  • Guanylate Cyclase / metabolism*
  • Protein Transport / physiology
  • Zebrafish / embryology*
  • Zebrafish / genetics
  • Zebrafish Proteins / genetics
  • Zebrafish Proteins / metabolism*
  • rab GTP-Binding Proteins / genetics
  • rab GTP-Binding Proteins / metabolism*

Substances

  • Cadherins
  • Zebrafish Proteins
  • mpp5a protein, zebrafish
  • rab11 protein
  • rab GTP-Binding Proteins
  • Guanylate Cyclase