E-cadherin supports steady-state Rho signaling at the epithelial zonula adherens

Priya, Rashmi, Yap, Alpha S. and Gomez, Guillermo A. (2013) E-cadherin supports steady-state Rho signaling at the epithelial zonula adherens. Differentiation, 86 3: 133-140. doi:10.1016/j.diff.2013.01.002

Author Priya, Rashmi
Yap, Alpha S.
Gomez, Guillermo A.
Title E-cadherin supports steady-state Rho signaling at the epithelial zonula adherens
Journal name Differentiation   Check publisher's open access policy
ISSN 0301-4681
Publication date 2013-10-01
Year available 2013
Sub-type Article (original research)
DOI 10.1016/j.diff.2013.01.002
Volume 86
Issue 3
Start page 133
End page 140
Total pages 8
Place of publication London, United Kingdom
Publisher Elsevier Ltd
Language eng
Formatted abstract
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.
Keyword E cadherin
Zonula adherens
Myosin II
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2014 Collection
Institute for Molecular Bioscience - Publications
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