Cooperative regulation of AJM-1 controls junctional integrity in Caenorhabditis elegans epithelia

Nat Cell Biol. 2001 Nov;3(11):983-91. doi: 10.1038/ncb1101-983.

Abstract

The function of epithelial cell sheets depends on the integrity of specialized cell-cell junctions that connect neighbouring cells. We have characterized the novel coiled-coil protein AJM-1, which localizes to an apical junctional domain of Caenorhabditis elegans epithelia basal to the HMR-HMP (cadherin-catenin) complex. In the absence of AJM-1, the integrity of this domain is compromised. Proper AJM-1 localization requires LET-413 and DLG-1, homologues of the Drosophila tumour suppressors Scribble and Discs large, respectively. DLG-1 physically interacts with AJM-1 and is required for its normal apical distribution, and LET-413 mediates the rapid accumulation of both DLG-1 and AJM-1 in the apical domain. In the absence of both dlg-1 and let-413 function AJM-1 is almost completely lost from apical junctions in embryos, whereas HMP-1 (alpha-catenin) localization is only mildly affected. We conclude that LET-413 and DLG-1 cooperatively control AJM-1 localization and that AJM-1 controls the integrity of a distinct apical junctional domain in C. elegans.

Publication types

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

MeSH terms

  • Animals
  • Base Sequence
  • Caenorhabditis elegans / embryology
  • Caenorhabditis elegans / genetics
  • Caenorhabditis elegans / metabolism
  • Caenorhabditis elegans / physiology*
  • Caenorhabditis elegans Proteins / genetics
  • Caenorhabditis elegans Proteins / metabolism*
  • Cell Polarity / physiology
  • DNA, Complementary
  • Epithelial Cells
  • Helminth Proteins / metabolism
  • Intercellular Junctions / physiology*
  • Molecular Sequence Data

Substances

  • AJM-1 protein, C elegans
  • Caenorhabditis elegans Proteins
  • DNA, Complementary
  • Helminth Proteins
  • LET-413 protein, C elegans

Associated data

  • GENBANK/AJ295228
  • GENBANK/U39650