Faculty Opinions recommendation of Beta-catenin N- and C-terminal tails modulate the coordinated binding of adherens junction proteins to beta-catenin.

Cadherin–catenin complexes, localized to adherens junctions, are essential for cell–cell adhesion. One means of regulating adhesion is through the juxtamembrane domain of the cadherin cytoplasmic tail. This region is the binding site for p120, leading to the hypothesis that p120 is a key regulator of cell adhesion. p120 has also been suggested to regulate the GTPase Rho and to regulate transcription via its binding partner Kaiso. To test these hypothesized functions, we turned to Drosophila, which has only a single p120 family member. It localizes to adherens junctions and binds the juxtamembrane region of DE-cadherin (DE-cad). We generated null alleles of p120 and found that mutants are viable and fertile and have no substantial changes in junction structure or function. However, p120 mutations strongly enhance mutations in the genes encoding DE-cadherin or Armadillo, the β-catenin homologue. Finally, we examined the localization of p120 during embryogenesis. p120 localizes to adherens junctions, but its localization there is less universal than that of core adherens junction proteins. Together, these data suggest that p120 is an important positive modulator of adhesion but that it is not an essential core component of adherens junctions.

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Ectopic expression of gastrokine 1 in gastric cancer cells up-regulates tight and adherens junction proteins network

Pathology - Research and Practice ◽

10.1016/j.prp.2015.04.008 ◽

2015 ◽

Vol 211 (8) ◽

pp. 577-583 ◽

Cited By ~ 10

Author(s):

Emilia Rippa ◽

Filomena Altieri ◽

Chiara Stella Di Stadio ◽

Giuseppina Miselli ◽

Annalisa Lamberti ◽

...

Keyword(s):

Gastric Cancer ◽

Cancer Cells ◽

Ectopic Expression ◽

Adherens Junction ◽

Gastric Cancer Cells ◽

Gastrokine 1 ◽

Adherens Junction Proteins ◽

Junction Proteins

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Altered expression and interaction of adherens junction proteins in the developing OLM of the Rho(−/−) mouse

Experimental Eye Research ◽

10.1016/j.exer.2007.08.004 ◽

2007 ◽

Vol 85 (5) ◽

pp. 714-720 ◽

Cited By ~ 12

Author(s):

Matthew Campbell ◽

Marian Humphries ◽

Paul Kenna ◽

Peter Humphries ◽

Brenda Brankin

Keyword(s):

Adherens Junction ◽

Altered Expression ◽

Adherens Junction Proteins ◽

Junction Proteins

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Regulation of Adherens Junction Dynamics by Phosphorylation Switches

Journal of Signal Transduction ◽

10.1155/2012/125295 ◽

2012 ◽

Vol 2012 ◽

pp. 1-14 ◽

Cited By ~ 26

Author(s):

Cristina Bertocchi ◽

Megha Vaman Rao ◽

Ronen Zaidel-Bar

Keyword(s):

Actin Cytoskeleton ◽

Enzymatic Activity ◽

Adherens Junctions ◽

Adherens Junction ◽

Adaptor Proteins ◽

Cell Junction ◽

Internal Forces ◽

Adherens Junction Proteins ◽

Junction Proteins

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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