Identification of plakoglobin domains required for association with N-cadherin and α-catenin

Paula A. Sacco, Tammy M. McGranahan, Margaret J. Wheelock, Keith R. Johnson

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127 Scopus citations

Abstract

Cadherins are calcium-dependent, cell surface glycoproteins involved in cell-cell adhesion. To function in cell-cell adhesion, the transmembrane cadherin molecule must be associated with the cytoskeleton via cytoplasmic proteins known as catenins. Three catenins, α-catenin, β-catenin, and γ-catenin (also known as plakoglobin), have been identified. The domain of the cadherin molecule important for its interaction with the catenins has been mapped to the COOH-terminal 70 amino acids, but less is known about regions of the catenins that allow them to associate with one another or with the cadherin molecule. In this study we have transfected carboxyl-terminal deletions of plakoglobin into the human fibrosarcoma HT-1080 and used immunofluorescence localization and co-immunoprecipitation to map the regions of plakoglobin that allow it to associate with N-cadherin and with α-catenin. Plakoglobin is an armadillo family member containing 13 weakly similar internal repeats. These data show that the α-catenin-binding region maps within the first repeat and the N-cadherin-binding region maps within repeats 7 and 8.

Original languageEnglish (US)
Pages (from-to)20201-20206
Number of pages6
JournalJournal of Biological Chemistry
Volume270
Issue number34
DOIs
StatePublished - Aug 25 1995

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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