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.
Highlights
Adherens junctions (AJs) are cell-cell adhesion sites where calcium-dependent cadherin receptors bind with their extracellular domains to cadherins on opposing cells and with their cytoplasmic tails connect—via adaptors—to filamentous actin [1, 2]
We address the question what are the ramifications of phosphorylation of AJ proteins on AJ structure and dynamics
From the examples presented above, it is clear that phosphorylation switches play a pivotal role in regulating AJ assembly and disassembly dynamics
Summary
Adherens junctions (AJs) are cell-cell adhesion sites where calcium-dependent cadherin receptors bind with their extracellular domains to cadherins on opposing cells and with their cytoplasmic tails connect—via adaptors—to filamentous actin [1, 2]. The ability of cells to regulate their adhesive interactions plays a key role during tissue morphogenesis, repair, and renewal [3, 7, 8]. Once a protein is expressed the cell can determine its localization by controlling its transport. Both exocytosis and endocytosis of Ecadherin are tightly controlled and the balance between the two processes has been shown to regulate AJ turnover both in vitro and in vivo [6]. A cell can control the activity and interactions of a protein at a given location by posttranslational modifications. These modifications include glycosylation, lipidation, ubiquitination, acetylation, proteolysis, and phosphorylation [11].
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