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Vol. 12, Issue 6, 1595-1609, June 2001
-Catenin-independent Recruitment of ZO-1 to Nectin-based
Cell-Cell Adhesion Sites through Afadin
and
*Department of Molecular Biology and Biochemistry and ZO-1 is an actin filament (F-actin)-binding protein that localizes
to tight junctions and connects claudin to the actin cytoskeleton in
epithelial cells. In nonepithelial cells that have no tight junctions,
ZO-1 localizes to adherens junctions (AJs) and may connect cadherin to
the actin cytoskeleton indirectly through Department
of Surgery and Clinical Oncology, Osaka University Graduate School of
Medicine/Faculty of Medicine, Suita 565-0871, Japan; and
§Department of Cell Biology, Faculty of Medicine, Kyoto
University, Kyoto 606-8501, Japan
- and 
-catenins as one
of many F-actin-binding proteins. Nectin is an immunoglobulin-like
adhesion molecule that localizes to AJs and is associated with the
actin cytoskeleton through afadin, an F-actin-binding protein. Ponsin
is an afadin- and vinculin-binding protein that also localizes to AJs.
The nectin-afadin complex has a potency to recruit the
E-cadherin--catenin complex through -catenin in a manner
independent of ponsin. By the use of cadherin-deficient L cell lines
stably expressing various components of the cadherin-catenin and
nectin-afadin systems, and -catenin-deficient F9 cell lines, we
examined here whether nectin recruits ZO-1 to nectin-based cell-cell
adhesion sites. Nectin showed a potency to recruit not only -catenin
but also ZO-1 to nectin-based cell-cell adhesion sites. This
recruitment of ZO-1 was dependent on afadin but independent of
-catenin and ponsin. These results indicate that ZO-1 localizes to
cadherin-based AJs through interactions not only with -catenin but
also with the nectin-afadin system.
These authors contributed equally to this work.
Corresponding author. E-mail address:
ytakai{at}molbio.med.osaka-u.ac.jp.
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