Presenilin-1 forms complexes with the cadherin/catenin cell-cell adhesion system and is recruited to intercellular and synaptic contacts

Mol Cell. 1999 Dec;4(6):893-902. doi: 10.1016/s1097-2765(00)80219-1.

Abstract

In MDCK cells, presenilin-1 (PS1) accumulates at intercellular contacts where it colocalizes with components of the cadherin-based adherens junctions. PS1 fragments form complexes with E-cadherin, beta-catenin, and alpha-catenin, all components of adherens junctions. In confluent MDCK cells, PS1 forms complexes with cell surface E-cadherin; disruption of Ca(2+)-dependent cell-cell contacts reduces surface PS1 and the levels of PS1-E-cadherin complexes. PS1 overexpression in human kidney cells enhances cell-cell adhesion. Together, these data show that PS1 incorporates into the cadherin/catenin adhesion system and regulates cell-cell adhesion. PS1 concentrates at intercellular contacts in epithelial tissue; in brain, it forms complexes with both E- and N-cadherin and concentrates at synaptic adhesions. That PS1 is a constituent of the cadherin/catenin complex makes that complex a potential target for PS1 FAD mutations.

Publication types

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

MeSH terms

  • Animals
  • Cadherins / metabolism*
  • Cell Adhesion
  • Cell Line
  • Cytoskeletal Proteins / metabolism
  • Dogs
  • Humans
  • Intercellular Junctions / metabolism*
  • Membrane Proteins / metabolism*
  • Presenilin-1
  • Rabbits
  • Synapses / metabolism*

Substances

  • Cadherins
  • Cytoskeletal Proteins
  • Membrane Proteins
  • PSEN1 protein, human
  • Presenilin-1