Isoform-specific differences in the size of desmosomal cadherin/catenin complexes

Leslie J. Bannon, Betty L. Cabrera, M. S. Stack, Kathleen J. Green

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

Via their integration of the intermediate filament cytoskeleton into the cell membrane, desmosomes facilitate the maintenance of cell shape and tissue integrity as well as intercellular communication. The transmembrane components of the desmosome, the desmogleins and desmocollins, are members of the cadherin family of cell-cell adhesion molecules. Each of these proteins exists as three distinct isoforms, which are the products of individual genes and expressed in a cell-type and differentiation-specific manner. Previous work has suggested that desmoglein 1 binds to its catenin partner, plakoglobin, in an approximately 6:1 stoichiometry. In this study, the molecular organization of complexes formed by plakoglobin and desmoglein 1, 2, or 3 are further examined through immunoprecipitation, size exclusion chromatography and sucrose density sedimentation analysis. It is shown that the complex formed between plakoglobin and desmoglein 1 has an overall molecular weight greater than that of plakoglobin/desmoglein 2 or plakoglobin/desmoglein 3; however, the stoichiometry of the plakoglobin/desmoglein 1 complex does not appear to exceed 2:1.

Original languageEnglish (US)
Pages (from-to)1302-1306
Number of pages5
JournalJournal of Investigative Dermatology
Volume117
Issue number5
DOIs
StatePublished - Nov 2001

Keywords

  • Desmocollin
  • Desmoglein
  • Plakoglobin

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Dermatology
  • Cell Biology

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