p120 catenin is essential for mesenchymal cadherin-mediated regulation of cell motility and invasiveness

Masahiro Yanagisawa, Panagiotis Z Anastasiadis

Research output: Contribution to journalArticle

99 Citations (Scopus)

Abstract

During epithelial tumor progression, the loss of E-cadherin expression and inappropriate expression of mesenchymal cadherins coincide with increased invasiveness. Reexpression experiments have established E-cadherin as an invasion suppressor. However, the mechanism by which E-cadherin suppresses invasiveness and the role of mesenchymal cadherins are poorly understood. We show that both p120 catenin and mesenchymal cadherins are required for the invasiveness of E-cadherin-deficient cells. p120 binding promotes the up-regulation of mesenchymal cadherins and the activation of Rac1, which are essential for cell migration and invasiveness. p120 also promotes invasiveness by inhibiting RhoA activity, independently of cadherin association. Furthermore, association of endogenous p120 with E-cadherin is required for E-cadherin-mediated suppression of invasiveness and is accompanied by a reduction in mesenchymal cadherin levels. The data indicate that p120 acts as a rheostat, promoting a sessile cellular phenotype when associated with E-cadherin or a motile phenotype when associated with mesenchymal cadherins.

Original languageEnglish (US)
Pages (from-to)1087-1096
Number of pages10
JournalJournal of Cell Biology
Volume174
Issue number7
DOIs
StatePublished - Sep 25 2006

Fingerprint

Cadherins
Cell Movement
delta catenin
Phenotype
Up-Regulation

ASJC Scopus subject areas

  • Cell Biology

Cite this

p120 catenin is essential for mesenchymal cadherin-mediated regulation of cell motility and invasiveness. / Yanagisawa, Masahiro; Anastasiadis, Panagiotis Z.

In: Journal of Cell Biology, Vol. 174, No. 7, 25.09.2006, p. 1087-1096.

Research output: Contribution to journalArticle

@article{867be13747e747139f3613f77dc51a3a,
title = "p120 catenin is essential for mesenchymal cadherin-mediated regulation of cell motility and invasiveness",
abstract = "During epithelial tumor progression, the loss of E-cadherin expression and inappropriate expression of mesenchymal cadherins coincide with increased invasiveness. Reexpression experiments have established E-cadherin as an invasion suppressor. However, the mechanism by which E-cadherin suppresses invasiveness and the role of mesenchymal cadherins are poorly understood. We show that both p120 catenin and mesenchymal cadherins are required for the invasiveness of E-cadherin-deficient cells. p120 binding promotes the up-regulation of mesenchymal cadherins and the activation of Rac1, which are essential for cell migration and invasiveness. p120 also promotes invasiveness by inhibiting RhoA activity, independently of cadherin association. Furthermore, association of endogenous p120 with E-cadherin is required for E-cadherin-mediated suppression of invasiveness and is accompanied by a reduction in mesenchymal cadherin levels. The data indicate that p120 acts as a rheostat, promoting a sessile cellular phenotype when associated with E-cadherin or a motile phenotype when associated with mesenchymal cadherins.",
author = "Masahiro Yanagisawa and Anastasiadis, {Panagiotis Z}",
year = "2006",
month = "9",
day = "25",
doi = "10.1083/jcb.200605022",
language = "English (US)",
volume = "174",
pages = "1087--1096",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "7",

}

TY - JOUR

T1 - p120 catenin is essential for mesenchymal cadherin-mediated regulation of cell motility and invasiveness

AU - Yanagisawa, Masahiro

AU - Anastasiadis, Panagiotis Z

PY - 2006/9/25

Y1 - 2006/9/25

N2 - During epithelial tumor progression, the loss of E-cadherin expression and inappropriate expression of mesenchymal cadherins coincide with increased invasiveness. Reexpression experiments have established E-cadherin as an invasion suppressor. However, the mechanism by which E-cadherin suppresses invasiveness and the role of mesenchymal cadherins are poorly understood. We show that both p120 catenin and mesenchymal cadherins are required for the invasiveness of E-cadherin-deficient cells. p120 binding promotes the up-regulation of mesenchymal cadherins and the activation of Rac1, which are essential for cell migration and invasiveness. p120 also promotes invasiveness by inhibiting RhoA activity, independently of cadherin association. Furthermore, association of endogenous p120 with E-cadherin is required for E-cadherin-mediated suppression of invasiveness and is accompanied by a reduction in mesenchymal cadherin levels. The data indicate that p120 acts as a rheostat, promoting a sessile cellular phenotype when associated with E-cadherin or a motile phenotype when associated with mesenchymal cadherins.

AB - During epithelial tumor progression, the loss of E-cadherin expression and inappropriate expression of mesenchymal cadherins coincide with increased invasiveness. Reexpression experiments have established E-cadherin as an invasion suppressor. However, the mechanism by which E-cadherin suppresses invasiveness and the role of mesenchymal cadherins are poorly understood. We show that both p120 catenin and mesenchymal cadherins are required for the invasiveness of E-cadherin-deficient cells. p120 binding promotes the up-regulation of mesenchymal cadherins and the activation of Rac1, which are essential for cell migration and invasiveness. p120 also promotes invasiveness by inhibiting RhoA activity, independently of cadherin association. Furthermore, association of endogenous p120 with E-cadherin is required for E-cadherin-mediated suppression of invasiveness and is accompanied by a reduction in mesenchymal cadherin levels. The data indicate that p120 acts as a rheostat, promoting a sessile cellular phenotype when associated with E-cadherin or a motile phenotype when associated with mesenchymal cadherins.

UR - http://www.scopus.com/inward/record.url?scp=33748997691&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33748997691&partnerID=8YFLogxK

U2 - 10.1083/jcb.200605022

DO - 10.1083/jcb.200605022

M3 - Article

C2 - 16982802

AN - SCOPUS:33748997691

VL - 174

SP - 1087

EP - 1096

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 7

ER -