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Published online 17 May 2004. doi:10.1083/jcb.200403006
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 165, Number 4, 517-528
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Article

Mammalian Fat1 cadherin regulates actin dynamics and cell–cell contact



Takuji Tanoue and Masatoshi Takeichi

RIKEN Center for Developmental Biology, Kobe 650-0047, Japan

Address correspondence to Masatoshi Takeichi, RIKEN Center for Developmental Biology, Minatojima-Minamimachi, Chuo-ku, Kobe 650-0047, Japan. Tel.: (81) 78-306-3116. Fax: (81) 78-306-3118. email: takeichi{at}cdb.riken.go.jp

Fat cadherins form a distinct subfamily of the cadherin gene superfamily, and are featured by their unusually large extracellular domain. In this work, we investigated the function of a mammalian Fat cadherin. Fat1 was localized at filopodial tips, lamellipodial edges, and cell–cell boundaries, overlapping with dynamic actin structures. RNA interference–mediated knockdown of Fat1 resulted in disorganization of cell junction–associated F-actin and other actin fibers/cables, disturbance of cell–cell contacts, and also inhibition of cell polarity formation at wound margins. Furthermore, we identified Ena/vasodilator-stimulated phosphoproteins as a potential downstream effector of Fat1. These results suggest that Fat1 regulates actin cytoskeletal organization at cell peripheries, thereby modulating cell contacts and polarity.

Key Words: Fat; cadherin; actin cytoskeleton; Ena/VASP; cell–cell interaction

The online version of this article includes supplemental material.

Abbreviations used in this paper: EC, extracellular cadherin; EVH1, Ena/VASP homology 1; Mena, mammalian Enabled; RNAi, RNA interference; VASP, vasodilator-stimulated phosphoprotein.


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