Involvement of protein phosphatase 2A in the maintenance of E-cadherin-mediated cell-cell adhesion through recruitment of IQGAP1.

Abstract:

:Serine/threonine protein phosphatase (PP) 2A regulates many biological processes, however it remains unclear whether PP2A participates in cadherin-mediated cell-cell adhesion. We show here that the core enzyme of PP2A (PP2A-AC) is localized in the cell-cell adhesion sites between adjacent cells and associated with the E-cadherin-catenins complex in non-malignant human mammary epithelial (HME) cells at confluence. Treatment of the cells with either okadaic acid (OA), an inhibitor of PP2A, or siRNA for the regulatory subunit A of PP2A (PP2A-A) caused disruption of cell-cell adhesion and F-actin assembly, without affecting the complex formation of E-cadherin with beta- and alpha-catenins. While a small GTPase Rac and its effector IQGAP1 were associated with the E-cadherin-catenins complex, either OA or PP2A-A siRNA concomitantly induced the dissociation of IQGAP1, but not Rac, from the complex and the internalization of E-cadherin from the cell surface. We therefore propose that PP2A plays a crucial role in the maintenance of cell-cell adhesion through recruitment of IQGAP1 to the Rac-bound E-cadherin-catenins complex.

journal_name

J Cell Physiol

authors

Takahashi K,Nakajima E,Suzuki K

doi

10.1002/jcp.20524

keywords:

subject

Has Abstract

pub_date

2006-03-01 00:00:00

pages

814-20

issue

3

eissn

0021-9541

issn

1097-4652

journal_volume

206

pub_type

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