期刊
DIFFERENTIATION
卷 86, 期 3, 页码 133-140出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.diff.2013.01.002
关键词
E-cadherin; Zonula adherens; Rho; ECT2; Centralspindlin; Myosin II
资金
- National Health and Medical Research Council [631377, 631383]
- Australian Research Council [DP120104667]
- Oncology Children's Foundation
- UQI (UQ International) Ph.D. Scholarship
- ANZ Trustees Ph.D. Scholarship in Medical Research
In simple polarized epithelial cells, the Rho GTPase commonly localizes to E-cadherin-based cell-cell junctions, such as the zonula adherens (ZA), where it regulates the actomyosin cytoskeleton to support junctional integrity and tension. An important question is how E-cadherin contributes to Rho signaling, notably whether junctional Rho may depend on cadherin adhesion. We sought to investigate this by assessing Rho localization and activity in epithelial monolayers depleted of E-cadherin by RNAi. We report that E-cadherin depletion reduced both Rho and Rho-GTP at the ZA, an effect that was rescued by expressing a RNAi-resistant full-length E-cadherin transgene. This impact on Rho signaling was accompanied by reduced junctional localization of the Rho GEF ECT2 and the centralspindlin complex that recruits ECT2. Further, the Rho signaling pathway contributes to the selective stabilization of E-cadherin molecules in the apical zone of the cells compared with E-cadherin at the lateral surface, thereby creating a more defined and restricted pool of E-cadherin that forms the ZA. Thus, E-cadherin and Rho signaling cooperate to ensure proper ZA architecture and function. (c) 2013 International Society of Differentiation. Published by Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据