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

Autoren

P Kussel-Andermann

DOI

10.1093/emboj/19.22.6020

eISSN

1460-2075

Ausgabe der Veröffentlichung

22

Zeitschrift

The EMBO Journal

Paginierung

6020 - 6029

Datum der Veröffentlichung

2000

Status

Published

Herausgeber

Springer Science and Business Media LLC

Herausgeber URL

http://dx.doi.org/10.1093/emboj/19.22.6020

Datum der Datenerfassung

2023

Titel

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

Ausgabe der Zeitschrift

19

Data source: Crossref

Abstract

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 alpha-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.

Addresses

Unité de Génétique des Déficits Sensoriels, CNRS URA 1968 and Unité des Interactions Bactéries-Cellules, Institut Pasteur, 25-28 rue du Dr Roux, 75724 Paris cedex 15, France.

Autoren

P Küssel-Andermann
A El-Amraoui
S Safieddine
S Nouaille
I Perfettini
M Lecuit
P Cossart
U Wolfrum
C Petit

DOI

10.1093/emboj/19.22.6020

eISSN

1460-2075

Externe Identifier

PubMed Identifier: 11080149
PubMed Central ID: PMC305826

Open access

false

ISSN

0261-4189

Ausgabe der Veröffentlichung

22

Zeitschrift

The EMBO journal

Schlüsselwörter

Cell Line
Intercellular Junctions
Animals
Humans
Mice
Deafness
Macromolecular Substances
Myosins
Cytoskeletal Proteins
Cadherins
Membrane Proteins
Alternative Splicing
Amino Acid Sequence
Protein Structure, Tertiary
Protein Binding
Mutation
Molecular Sequence Data
alpha Catenin
Hair Cells, Auditory
Dyneins
In Vitro Techniques
Myosin VIIa

Sprache

eng

Medium

Print

Paginierung

6020 - 6029

Datum der Veröffentlichung

2000

Status

Published

Datum der Datenerfassung

2000

Titel

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

Sub types

Research Support, Non-U.S. Gov't
research-article
Journal Article

Ausgabe der Zeitschrift

19

Data source: Europe PubMed Central

Abstract

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 alpha-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.

Autoren

P Küssel-Andermann
A El-Amraoui
S Safieddine
S Nouaille
I Perfettini
M Lecuit
P Cossart
U Wolfrum
C Petit

Autoren-URL

https://www.ncbi.nlm.nih.gov/pubmed/11080149

DOI

10.1093/emboj/19.22.6020

Externe Identifier

PubMed Central ID: PMC305826

ISSN

0261-4189

Ausgabe der Veröffentlichung

22

Zeitschrift

EMBO J

Schlüsselwörter

Alternative Splicing
Amino Acid Sequence
Animals
Cadherins
Cell Line
Cytoskeletal Proteins
Deafness
Dyneins
Hair Cells, Auditory
Humans
In Vitro Techniques
Intercellular Junctions
Macromolecular Substances
Membrane Proteins
Mice
Molecular Sequence Data
Mutation
Myosin VIIa
Myosins
Protein Binding
Protein Structure, Tertiary
alpha Catenin

Sprache

eng

Country

England

Paginierung

6020 - 6029

Datum der Veröffentlichung

2000

Status

Published

Datum, an dem der Datensatz öffentlich gemacht wurde

2001

Titel

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

Sub types

Journal Article
Research Support, Non-U.S. Gov't

Ausgabe der Zeitschrift

19

Data source: PubMed

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

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