Desmocollin-2 alone forms functional desmosomal plaques, with the plaque formation requiring the juxtamembrane region and plakophilins

J Biochem. 2015 Oct;158(4):339-53. doi: 10.1093/jb/mvv048. Epub 2015 May 13.

Abstract

The role of the juxtamembrane region of the desmocollin-2 cytoplasmic domain in desmosome formation was investigated by using gene knockout and reconstitution experiments. When a deletion construct of the desmocollin-2 juxtamembrane region was expressed in HaCaT cells, the mutant protein became localized linearly at the cell-cell boundary, suggesting the involvement of this region in desmosomal plaque formation. Then, desmocollin-2 and desmoglein-2 genes of epithelial DLD-1 cells were ablated by using the CRISPR/Cas9 system. The resultant knockout cells did not form desmosomes, but re-expression of desmocollin-2 in the cells formed desmosomal plaques in the absence of desmoglein-2 and the transfectants showed significant cell adhesion activity. Intriguingly, expression of desmocollin-2 lacking its juxtamembrane region did not form the plaques. The results of an immunoprecipitation and GST-fusion protein pull-down assay suggested the binding of plakophilin-2 and -3 to the region. Ablation of plakophilin-2 and -3 genes resulted in disruption of the plaque-like accumulation and linear localization of desmocollin-2 at intercellular contact sites. These results suggest that the juxtamembrane region of desmocollin-2 and plakophilins are involved in the desmosomal plaque formation, possibly through the interaction between this region and plakophilins.

Keywords: CRISPR; Cas9; DLD-1 cells; desmocollin-2; desmosome; juxtamembrane domain; knockout; plakophilin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigens, CD
  • CRISPR-Cas Systems
  • Cadherins / chemistry
  • Cadherins / genetics
  • Cadherins / metabolism
  • Cell Adhesion
  • Cell Line, Tumor
  • Desmocollins / antagonists & inhibitors
  • Desmocollins / chemistry
  • Desmocollins / genetics
  • Desmocollins / metabolism*
  • Desmoglein 2 / antagonists & inhibitors
  • Desmoglein 2 / chemistry
  • Desmoglein 2 / genetics
  • Desmoglein 2 / metabolism
  • Desmosomes / metabolism*
  • Desmosomes / ultrastructure
  • Epithelial Cells / metabolism*
  • Epithelial Cells / ultrastructure
  • Gene Deletion
  • Humans
  • Immunoprecipitation
  • Microscopy, Electron, Transmission
  • Microscopy, Fluorescence
  • Mutant Proteins / antagonists & inhibitors
  • Mutant Proteins / chemistry
  • Mutant Proteins / metabolism
  • Peptide Fragments / antagonists & inhibitors
  • Peptide Fragments / chemistry
  • Peptide Fragments / genetics
  • Peptide Fragments / metabolism
  • Plakophilins / antagonists & inhibitors
  • Plakophilins / chemistry
  • Plakophilins / genetics
  • Plakophilins / metabolism*
  • Protein Interaction Domains and Motifs
  • Recombinant Fusion Proteins
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism

Substances

  • Antigens, CD
  • CDH1 protein, human
  • Cadherins
  • DSC2 protein, human
  • DSG2 protein, human
  • Desmocollins
  • Desmoglein 2
  • Mutant Proteins
  • PKP2 protein, human
  • PKP3 protein, human
  • Peptide Fragments
  • Plakophilins
  • Recombinant Fusion Proteins
  • Recombinant Proteins