Vezatin, a novel transmembrane protein, bridges myosin VIIA to the cadherin-catenins complex

6533b860fe1ef96bd12c318a

RESEARCH PRODUCT

Vezatin, a novel transmembrane protein, bridges myosin VIIA to the cadherin-catenins complex

Uwe Wolfrum Aziz El-amraoui Marc Lecuit Christine Petit Saaid Safieddine Isabelle Perfettini Polonca Küssel-andermann Pascale Cossart Sylvie Nouaille

subject

MESH: Cytoskeletal Proteins MESH: alpha Catenin Stereocilia (inner ear)[SDV]Life Sciences [q-bio]MESH: Amino Acid Sequence Deafness MESH: Cadherins Mice MESH: Protein Structure Tertiary 0302 clinical medicine [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases Myosin MESH: Hair Cells Auditory MESH: Animals Cytoskeleton 0303 health sciences FERM domain General Neuroscience MESH: Alternative Splicing Articles Cadherins Cell biology medicine.anatomical_structure Intercellular Junctions [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology Myosin VIIa Hair cell MESH: Membrane Proteins MESH: Dyneins Protein Binding MESH: Mutation Macromolecular Substances Molecular Sequence Data MESH: Deafness macromolecular substances Biology In Vitro Techniques Myosins General Biochemistry Genetics and Molecular Biology Cell Line Adherens junction 03 medical and health sciences Hair Cells Auditory medicine otorhinolaryngologic diseases Animals Humans MESH: Myosin VIIa MESH: Protein Binding Amino Acid Sequence Molecular Biology MESH: Mice 030304 developmental biology MESH: In Vitro Techniques MESH: Molecular Sequence Data MESH: Humans General Immunology and Microbiology Cadherin Dyneins Membrane Proteins MESH: Macromolecular Substances MESH: Myosins Actin cytoskeleton [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology Protein Structure Tertiary MESH: Cell Line Alternative Splicing Cytoskeletal Proteins Mutation sense organs 030217 neurology & neurosurgery alpha Catenin [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology MESH: Intercellular Junctions

description

International audience; 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 identi®ed 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 a-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 ®brillar 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.

year	journal	country	edition	language
2000-11-01

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