α-Catenin contributes to the strength of E-cadherin-p120 interactions

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α-Catenin contributes to the strength of E-cadherin-p120 interactions. / Troyanovsky, Regina B; Klingelhöfer, Jörg; Troyanovsky, Sergey M.

I: Molecular Biology of the Cell, Bind 22, Nr. 22, 11.2011, s. 4247-55.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning

Harvard

Troyanovsky, RB, Klingelhöfer, J & Troyanovsky, SM 2011, 'α-Catenin contributes to the strength of E-cadherin-p120 interactions', Molecular Biology of the Cell, bind 22, nr. 22, s. 4247-55. https://doi.org/10.1091/mbc.E11-03-0250

APA

Troyanovsky, R. B., Klingelhöfer, J., & Troyanovsky, S. M. (2011). α-Catenin contributes to the strength of E-cadherin-p120 interactions. Molecular Biology of the Cell, 22(22), 4247-55. https://doi.org/10.1091/mbc.E11-03-0250

Vancouver

Troyanovsky RB, Klingelhöfer J, Troyanovsky SM. α-Catenin contributes to the strength of E-cadherin-p120 interactions. Molecular Biology of the Cell. 2011 nov.;22(22):4247-55. https://doi.org/10.1091/mbc.E11-03-0250

Author

Troyanovsky, Regina B ; Klingelhöfer, Jörg ; Troyanovsky, Sergey M. / α-Catenin contributes to the strength of E-cadherin-p120 interactions. I: Molecular Biology of the Cell. 2011 ; Bind 22, Nr. 22. s. 4247-55.

Bibtex

@article{1e7e9f4565134792a81521adf9b3cd57,
title = "α-Catenin contributes to the strength of E-cadherin-p120 interactions",
abstract = "Cadherin-catenin interactions play an important role in cadherin-mediated adhesion. Here we present strong evidence that in the cadherin-catenin complex α-catenin contributes to the binding strength of another catenin, p120, to the same complex. Specifically, we found that a β-catenin-uncoupled cadherin mutant interacts much more weakly with p120 than its full-size counterpart and that it is rapidly endocytosed from the surface of A-431 cells. We also showed that p120 overexpression stabilizes this mutant on the cell surface. Examination of the α-catenin-deficient MDA-MB-468 cells and their derivates in which α-catenin was reintroduced showed that α-catenin reinforces E-cadherin-p120 association. Finally, a cross-linking analysis of the cadherin-catenin complex indicated that a large loop located in the middle of the p120 arm-repeat domain is in close spatial vicinity to the amino-terminal VH1 domain of α-catenin. The six amino acid-long extension of this loop, caused by an alternative splicing, weakens p120 binding to cadherin. The data suggest that α-catenin-p120 contact within the cadherin-catenin complex can regulate cadherin trafficking.",
keywords = "Cadherins, Catenins, Cell Adhesion, Cell Adhesion Molecules, Cell Line, Tumor, Cell Membrane, Humans, Mutation, Protein Binding, Protein Transport, Signal Transduction, alpha Catenin, beta Catenin",
author = "Troyanovsky, {Regina B} and J{\"o}rg Klingelh{\"o}fer and Troyanovsky, {Sergey M}",
year = "2011",
month = nov,
doi = "10.1091/mbc.E11-03-0250",
language = "English",
volume = "22",
pages = "4247--55",
journal = "Molecular Biology of the Cell",
issn = "1059-1524",
publisher = "American Society for Cell Biology",
number = "22",

}

RIS

TY - JOUR

T1 - α-Catenin contributes to the strength of E-cadherin-p120 interactions

AU - Troyanovsky, Regina B

AU - Klingelhöfer, Jörg

AU - Troyanovsky, Sergey M

PY - 2011/11

Y1 - 2011/11

N2 - Cadherin-catenin interactions play an important role in cadherin-mediated adhesion. Here we present strong evidence that in the cadherin-catenin complex α-catenin contributes to the binding strength of another catenin, p120, to the same complex. Specifically, we found that a β-catenin-uncoupled cadherin mutant interacts much more weakly with p120 than its full-size counterpart and that it is rapidly endocytosed from the surface of A-431 cells. We also showed that p120 overexpression stabilizes this mutant on the cell surface. Examination of the α-catenin-deficient MDA-MB-468 cells and their derivates in which α-catenin was reintroduced showed that α-catenin reinforces E-cadherin-p120 association. Finally, a cross-linking analysis of the cadherin-catenin complex indicated that a large loop located in the middle of the p120 arm-repeat domain is in close spatial vicinity to the amino-terminal VH1 domain of α-catenin. The six amino acid-long extension of this loop, caused by an alternative splicing, weakens p120 binding to cadherin. The data suggest that α-catenin-p120 contact within the cadherin-catenin complex can regulate cadherin trafficking.

AB - Cadherin-catenin interactions play an important role in cadherin-mediated adhesion. Here we present strong evidence that in the cadherin-catenin complex α-catenin contributes to the binding strength of another catenin, p120, to the same complex. Specifically, we found that a β-catenin-uncoupled cadherin mutant interacts much more weakly with p120 than its full-size counterpart and that it is rapidly endocytosed from the surface of A-431 cells. We also showed that p120 overexpression stabilizes this mutant on the cell surface. Examination of the α-catenin-deficient MDA-MB-468 cells and their derivates in which α-catenin was reintroduced showed that α-catenin reinforces E-cadherin-p120 association. Finally, a cross-linking analysis of the cadherin-catenin complex indicated that a large loop located in the middle of the p120 arm-repeat domain is in close spatial vicinity to the amino-terminal VH1 domain of α-catenin. The six amino acid-long extension of this loop, caused by an alternative splicing, weakens p120 binding to cadherin. The data suggest that α-catenin-p120 contact within the cadherin-catenin complex can regulate cadherin trafficking.

KW - Cadherins

KW - Catenins

KW - Cell Adhesion

KW - Cell Adhesion Molecules

KW - Cell Line, Tumor

KW - Cell Membrane

KW - Humans

KW - Mutation

KW - Protein Binding

KW - Protein Transport

KW - Signal Transduction

KW - alpha Catenin

KW - beta Catenin

U2 - 10.1091/mbc.E11-03-0250

DO - 10.1091/mbc.E11-03-0250

M3 - Journal article

C2 - 21937720

VL - 22

SP - 4247

EP - 4255

JO - Molecular Biology of the Cell

JF - Molecular Biology of the Cell

SN - 1059-1524

IS - 22

ER -

ID: 61726201