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First published online May 28, 2005
doi: 10.1242/10.1242/jcs.02398

Journal of Cell Science 118, 2347-2353 (2005)
Published by The Company of Biologists 2005
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Commentary

New insights into Fat cadherins

Takuji Tanoue and Masatoshi Takeichi*

RIKEN Center for Developmental Biology, Minatojima-Minamimachi, Chuo-ku, Kobe 650-0047, Japan

* Author for correspondence (e-mail: takeichi{at}cdb.riken.go.jp)

Cell-cell adhesion is fundamental to multicellular architecture. Several classes of adhesion molecule are used to achieve this, and cadherins represent a major family of such molecules. The cadherin family has multiple subfamilies. Members of the Fat cadherin subfamily, which is conserved across species, have an extraordinarily large extracellular region, comprising 34 repeated domains, making them the largest cadherin molecules. Classic Fat, identified in Drosophila, is known to regulate cell proliferation and planar cell polarity. Recent studies of one of its mammalian homologs, Fat1, have revealed novel functions of this molecule. Fat1 binds to Ena/VASP proteins and regulates actin dynamics at both cell-cell contacts and leading edges. These observations suggest that Fat1 is an important regulator of actin dynamics and controls cell-cell interactions through this activity.

Key words: Fat, Cadherin, Cell-cell interaction, Actin dynamics




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© The Company of Biologists Ltd 2005