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MBC in Press, published online ahead of print September 29, 2004
Mol. Biol. Cell 10.1091/mbc.E04-04-0350

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Submitted on April 29, 2004
Revised on September 3, 2004
Accepted on September 16, 2004

Association of ARVCF with ZO-1 and ZO-2: Binding to PDZ-Domain Proteins and Cell-Cell Adhesion Regulate Plasma Membrane and Nuclear Localization of ARVCF

P. Jaya Kausalya, Dominic C. Y. Phua, and Walter Hunziker*

Institute of Molecular and Cell Biology, Epithelial Cell Biology Laboratory, Singapore 138673, Singapore

Monitoring Editor: Keith Mostov

ARVCF, an armadillo-repeat protein of the p120ctn family, associates with classical cadherins and is present in adherens junctions but its function is poorly understood. Here we show that ARVCF interacts via a C-terminal PDZ-binding motif with ZO-1 and ZO-2. ARVCF and ZO-1 partially colocalize in the vicinity of the apical adhesion complex in polarized epithelial MDCK cells. ARVCF, ZO-1 and E-cadherin form a complex and are recruited to sites of initial cell-cell contact in sparse cell cultures. E-cadherin binding and plasma membrane localization of ARVCF require the PDZ-binding motif. Disruption of cell-cell adhesion releases ARVCF from the plasma membrane and an increased fraction of the protein localizes to the nucleus. Nuclear localization of ARVCF also requires the PDZ-binding motif and can be mediated by the PDZ domains of ZO-2. Thus, the interaction of ARVCF with distinct PDZ-domain proteins determines its subcellular localization. Interactions with ZO-1 and ZO-2, in particular, may mediate recruitment of ARVCF to the plasma membrane and the nucleus, respectively, possibly in response to cell-cell adhesion cues.

*Corresponding author. E-mail: Hunziker{at}imcb.a-star.edu.sg






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