Premium
Vezatin, a novel transmembrane protein, bridges myosin VIIA to the cadherin–catenins complex
Author(s) -
KüsselAndermann Polonca,
ElAmraoui Aziz,
Safieddine Saaid,
Nouaille Sylvie,
Perfettini Isabelle,
Lecuit Marc,
Cossart Pascale,
Wolfrum Uwe,
Petit Christine
Publication year - 2000
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/19.22.6020
Subject(s) - adherens junction , biology , microbiology and biotechnology , stereocilia (inner ear) , myosin , cadherin , catenin , transmembrane protein , hair cell , cell , biochemistry , anatomy , cochlea , signal transduction , wnt signaling pathway , receptor
Defects in myosin VIIA are responsible for deafness in the human and mouse. The role of this unconventional myosin in the sensory hair cells of the inner ear is not yet understood. Here we show that the C‐terminal FERM domain of myosin VIIA binds to a novel transmembrane protein, vezatin, which we identified by a yeast two‐hybrid screen. Vezatin is a ubiquitous protein of adherens cell–cell junctions, where it interacts with both myosin VIIA and the cadherin–catenins complex. Its recruitment to adherens junctions implicates the C‐terminal region of α‐catenin. Taken together, these data suggest that myosin VIIA, anchored by vezatin to the cadherin–catenins complex, creates a tension force between adherens junctions and the actin cytoskeleton that is expected to strengthen cell–cell adhesion. In the inner ear sensory hair cells vezatin is, in addition, concentrated at another membrane–membrane interaction site, namely at the fibrillar links interconnecting the bases of adjacent stereocilia. In myosin VIIA‐defective mutants, inactivity of the vezatin–myosin VIIA complex at both sites could account for splaying out of the hair cell stereocilia.