E-cadherin dis-engagement activates the Rap1 GTPase

Sirisha Asuri, Jingliang Yan, Nivanka C. Paranavitana, Lawrence A. Quilliam

Research output: Contribution to journalArticle

36 Scopus citations

Abstract

E-cadherin based adherens junctions are finely regulated by multiple cellular signaling events. Here we show that the Ras-related Rap1 GTPase is enriched in regions of nascent cell-cell contacts and strengthens E-cadherin junctions: constitutively active Rap1 expressing MDCK cells exhibit increased junctional contact and resisted calcium depletion-induced cell-cell junction disruption. E-cadherin disengagement activated Rap1 and this correlated with E-cadherin association with the Rap GEFs, C3G and PDZ-GEF I. PDZ-GEF I associated with E-cadherin and β-catenin whereas C3G interaction with E-cadherin did not involve β-catenin. Knockdown of PDZ-GEF I in MDCK cells decreased Rap1 activity following E-cadherin junction disruption. We hereby show that Rap1 plays a role in the maintenance and repair of E-cadherin junctions and is activated via an "outside-in" signaling pathway initiated by E-cadherin and mediated at least in part by PDZ-GEF I.

Original languageEnglish (US)
Pages (from-to)1027-1037
Number of pages11
JournalJournal of Cellular Biochemistry
Volume105
Issue number4
DOIs
StatePublished - Jan 11 2008

Keywords

  • Adherens junction
  • C3G
  • E-cadherin
  • Guanine nucleotide exchange factor
  • PDZ-GEF
  • Rap1

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

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