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. 2012:2012:125295.
doi: 10.1155/2012/125295. Epub 2012 Jul 12.

Regulation of adherens junction dynamics by phosphorylation switches

Cristina Bertocchi  1 , Megha Vaman Rao, Ronen Zaidel-Bar
Affiliations

Regulation of adherens junction dynamics by phosphorylation switches

Cristina Bertocchi et al. J Signal Transduct. 2012.

Abstract

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.

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Figures

Figure 1
Figure 1
Network of phosphorylation enzymes and targets in the adherens junction.
See this image and copyright information in PMC

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