Drosophila α-catenin and E-cadherin bind to distinct regions of Drosophila Armadillo

L. M. Pai, C. Kirkpatrick, J. Blanton, H. Oda, M. Takeichi, M. Peifer

Research output: Contribution to journalArticlepeer-review

82 Scopus citations

Abstract

Adherens junctions are multiprotein complexes mediating cell-cell adhesion and communication. They are organized around a transmembrane cadherin, which binds a set of cytoplasmic proteins required for adhesion and to link the complex to the actin cytoskeleton. Three components of Drosophila adherens junctions, analogous to those in vertebrates, have been identified: Armadillo (homolog of β-catenin), Drosophila E-cadherin (DE-cadherin), and α-catenin. We carried out the first analysis of the interactions between these proteins using in vitro binding assays, the yeast two-hybrid system, and in vivo assays. We identified a 76-amino acid region of Armadillo that is necessary and sufficient for binding α-catenin and found that the N- terminal 258 amino acids of α-catenin interact with Armadillo. A large region of Armadillo, spanning six central Armadillo repeats, is required for DE-cadherin binding, whereas only 41 amino acids of the DE-cadherin cytoplasmic tail are sufficient for Armadillo binding. Our data complement and extend results obtained in studies of vertebrate adherens junctions, providing a foundation for understanding how junctional proteins assemble and a basis for interpreting existing mutations and creating new ones.

Original languageEnglish (US)
Pages (from-to)32411-32420
Number of pages10
JournalJournal of Biological Chemistry
Volume271
Issue number50
DOIs
StatePublished - 1996
Externally publishedYes

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