title: New insights into Fat cadherins.
abstract: 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.
authors.affiliation: RIKEN Center for Developmental Biology, Minatojima-Minamimachi, Chuo-ku, Kobe 650-0047, Japan.
authors.forename: Takuji
authors.initials: T
authors.lastname: Tanoue
authors.forename: Masatoshi
authors.initials: M
authors.lastname: Takeichi
mesh_terms: D000199:Actins / Q000378:metabolism; D000818:Animals; D015820:Cadherins / Q000378:metabolism*; D049109:Cell Proliferation; D004268:DNA-Binding Proteins / Q000378:metabolism*; D006801:Humans; D007365:Intercellular Junctions / Q000378:metabolism; D011485:Protein Binding / Q000502:physiology
chemical_list: D000199:Actins; D015820:Cadherins; D004268:DNA-Binding Proteins; C092744:ENA-VASP proteins; C502403:FAT1 protein, human