Characterization of the interactions of α-catenin with α-actinin and β-catenin/plakoglobin

Jill E. Nieset, Ann R. Redfield, Fang Jin, Karen A. Knudsen, Keith R. Johnson, Margaret J. Wheelock

Research output: Contribution to journalArticlepeer-review

229 Scopus citations


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. β-catenin or plakoglobin is associated directly with the cadherin; α-catenin binds to β-catenin/plakoglobin and serves to link the cadherin/catenin complex to the actin cytoskeleton. The domains on the cadherin and β-catenin/plakoglobin that are responsible for protein-protein interactions have been mapped. However, little is known about the molecular interactions between α-catenin and β-catenin/plakoglobin or about the interactions between α-catenin and the cytoskeleton. In this study we have used the yeast two-hybrid system to map the domains on α-catenin that allow it to associate with β-catenin/plakoglobin and with α-actinin. We also identify a region on α-actinin that is responsible for its interaction with α-catenin. The yeast two-hybrid data were confirmed with biochemical studies.

Original languageEnglish (US)
Pages (from-to)1013-1022
Number of pages10
JournalJournal of cell science
Issue number8
StatePublished - 1997
Externally publishedYes


  • Cadherin
  • Cytoskeleton
  • Plakoglobin
  • α-actinin
  • α-catenin
  • β-catenin

ASJC Scopus subject areas

  • Cell Biology


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