Table of Contents
Journal of Signal Transduction
Volume 2012 (2012), Article ID 125295, 14 pages
Review Article

Regulation of Adherens Junction Dynamics by Phosphorylation Switches

1Mechanobiology Institute Singapore, National University of Singapore, Singapore 117411
2Department of Bioengineering, Faculty of Engineering, National University of Singapore, Singapore 119077

Received 5 March 2012; Revised 21 May 2012; Accepted 22 May 2012

Academic Editor: Donna Webb

Copyright © 2012 Cristina Bertocchi et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Adherens junctions connect the actin cytoskeleton of neighboring cells through transmembrane cadherin receptors and a network of adaptor proteins. The interactions between these adaptors and cadherin as well as the activity of actin regulators localized to adherens junctions are tightly controlled to facilitate cell junction assembly or disassembly in response to changes in external or internal forces and/or signaling. Phosphorylation of tyrosine, serine, or threonine residues acts as a switch on the majority of adherens junction proteins, turning “on” or “off” their interactions with other proteins and/or their enzymatic activity. Here, we provide an overview of the kinases and phosphatases regulating phosphorylation of adherens junction proteins and bring examples of phosphorylation events leading to the assembly or disassembly of adherens junctions, highlighting the important role of phosphorylation switches in regulating their dynamics.