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The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
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E-cadherin interactome complexity and robustness resolved by quantitative proteomics.

Zhenhuan Guo1, Lisa J Neilson2, Hang Zhong1

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This study reveals the proteins interacting with E-cadherin

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • E-cadherin is crucial for epithelial tissue integrity and signaling.
  • Its function relies on extracellular domains and intracellular adaptors.
  • Understanding its interactome is key to epithelial biology.

Purpose of the Study:

  • To comprehensively map proteins interacting with E-cadherin's cytoplasmic tail.
  • To characterize the E-cadherin interactome and its cellular localization.
  • To investigate the dependence of intracellular interactions on cell-cell adhesion.

Main Methods:

  • Proximity biotinylation and quantitative proteomics to identify E-cadherin interactors.
  • Proteomics of adhesion plaques and GFP tagging for subcellular localization.
  • Construction of a comprehensive E-cadherin interaction network.

Main Results:

  • Identified 561 proteins near E-cadherin's cytoplasmic tail.
  • Characterized the localization of 83 proteins, including 24 novel adherens junction proteins.
  • Built a network of 79 published and 394 uncharacterized proteins.
  • Found most intracellular interactions are independent of extracellular E-cadherin binding.

Conclusions:

  • The E-cadherin interactome is extensive and includes novel components.
  • Subcellular localization data refines understanding of E-cadherin complex organization.
  • Intracellular E-cadherin interactions are largely independent of cell-cell adhesion, suggesting alternative regulatory mechanisms.