scholarly journals Drosophila p120catenin plays a supporting role in cell adhesion but is not an essential adherens junction component

2003 ◽  
Vol 160 (3) ◽  
pp. 433-449 ◽  
Author(s):  
Steven H. Myster ◽  
Robert Cavallo ◽  
Charles T. Anderson ◽  
Donald T. Fox ◽  
Mark Peifer
Keyword(s):  
Cell Adhesion ◽  
Adherens Junctions ◽  
Adherens Junction ◽  
Null Alleles ◽  
Juxtamembrane Region ◽  
Genes Encoding ◽  
Positive Modulator ◽  
Adherens Junction Proteins ◽  
Junction Structure ◽  
Junction Proteins

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.

scholarly journals Regulation of Adherens Junction Dynamics by Phosphorylation Switches

2012 ◽  
Vol 2012 ◽  
pp. 1-14 ◽  
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.

scholarly journals The Protein Tyrosine Phosphatase Pez Is a Major Phosphatase of Adherens Junctions and Dephosphorylates β-Catenin

2003 ◽  
Vol 14 (6) ◽  
pp. 2520-2529 ◽  
Author(s):  
Carol Wadham ◽  
Jennifer R Gamble ◽  
Mathew A Vadas ◽  
Yeesim Khew-Goodall
Keyword(s):  
Cell Adhesion ◽  
Tyrosine Phosphorylation ◽  
Adherens Junctions ◽  
Tyrosine Phosphatase ◽  
Adherens Junction ◽  
Dominant Negative ◽  
Dominant Negative Mutant ◽  
Adherens Junction Proteins ◽  
Cell Cell

Cell-cell adhesion regulates processes important in embryonal development, normal physiology, and cancer progression. It is regulated by various mechanisms including tyrosine phosphorylation. We have previously shown that the protein tyrosine phosphatase Pez is concentrated at intercellular junctions in confluent, quiescent monolayers but is nuclear in cells lacking cell-cell contacts. We show here with an epithelial cell model that Pez localizes to the adherens junctions in confluent monolayers. A truncation mutant lacking the catalytic domain acts as a dominant negative mutant to upregulate tyrosine phosphorylation at adherens junctions. We identified β-catenin, a component of adherens junctions, as a substrate of Pez by a “substrate trapping” approach and by in vitro dephosphorylation with recombinant Pez. Consistent with this, ectopic expression of the dominant negative mutant caused an increase in tyrosine phosphorylation of β-catenin, demonstrating that Pez regulates the level of tyrosine phosphorylation of adherens junction proteins, including β-catenin. Increased tyrosine phosphorylation of adherens junction proteins has been shown to decrease cell-cell adhesion, promoting cell migration as a result. Accordingly, the dominant negative Pez mutant enhanced cell motility in an in vitro “wound” assay. This suggests that Pez is also a regulator of cell motility, most likely through its action on cell-cell adhesion.

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

2015 ◽  
Vol 211 (8) ◽  
pp. 577-583 ◽  
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

scholarly journals Minus end–directed motor KIFC3 suppresses E-cadherin degradation by recruiting USP47 to adherens junctions

2014 ◽  
Vol 25 (24) ◽  
pp. 3851-3860 ◽  
Author(s):  
Kyoko Sako-Kubota ◽  
Nobutoshi Tanaka ◽  
Shigenori Nagae ◽  
Wenxiang Meng ◽  
Masatoshi Takeichi
Keyword(s):  
Cell Adhesion ◽  
Proteasome Inhibitors ◽  
Adherens Junction ◽  
Ubiquitin Protein Ligase ◽  
Juxtamembrane Region ◽  
Specific Protease ◽  
Ubiquitin Specific Protease ◽  
Epithelial Sheets ◽  
E Cadherin ◽  
Cell Cell

The adherens junction (AJ) plays a crucial role in maintaining cell–cell adhesion in epithelial tissues. Previous studies show that KIFC3, a minus end–directed kinesin motor, moves into AJs via microtubules that grow from clusters of CAMSAP3 (also known as Nezha), a protein that binds microtubule minus ends. The function of junction-associated KIFC3, however, remains to be elucidated. Here we find that KIFC3 binds the ubiquitin-specific protease USP47, a protease that removes ubiquitin chains from substrates and hence inhibits proteasome-mediated proteolysis, and recruits it to AJs. Depletion of KIFC3 or USP47 promotes cleavage of E-cadherin at a juxtamembrane region of the cytoplasmic domain, resulting in the production of a 90-kDa fragment and the internalization of E-cadherin. This cleavage depends on the E3 ubiquitin protein ligase Hakai and is inhibited by proteasome inhibitors. E-cadherin ubiquitination consistently increases after depletion of KIFC3 or USP47. These findings suggest that KIFC3 suppresses the ubiquitination and resultant degradation of E-cadherin by recruiting USP47 to AJs, a process that may be involved in maintaining stable cell–cell adhesion in epithelial sheets.

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

2007 ◽  
Vol 85 (5) ◽  
pp. 714-720 ◽  
Author(s):  
Matthew Campbell ◽  
Marian Humphries ◽  
Paul Kenna ◽  
Peter Humphries ◽  
Brenda Brankin
Keyword(s):  
Adherens Junction ◽  
Altered Expression ◽  
Adherens Junction Proteins ◽  
Junction Proteins

scholarly journals Enhanced interaction between focal adhesion and adherens junction proteins: Involvement in sphingosine 1-phosphate-induced endothelial barrier enhancement

2009 ◽  
Vol 77 (3) ◽  
pp. 304-313 ◽  
Author(s):  
Xiaoguang Sun ◽  
Yasushi Shikata ◽  
Lichun Wang ◽  
Kazuyoshi Ohmori ◽  
Naoko Watanabe ◽  
...  
Keyword(s):  
Focal Adhesion ◽  
Adherens Junction ◽  
Endothelial Barrier ◽  
Sphingosine 1 Phosphate ◽  
Adherens Junction Proteins ◽  
Junction Proteins

scholarly journals Avian Podocytes, Which Lack Nephrin, Use Adherens Junction Proteins at Intercellular Junctions

2015 ◽  
Vol 64 (1) ◽  
pp. 67-76 ◽  
Author(s):  
Eishin Yaoita ◽  
Hiroko Nishimura ◽  
Masaaki Nameta ◽  
Yutaka Yoshida ◽  
Hiroki Takimoto ◽  
...  
Keyword(s):  
Adherens Junction ◽  
Intercellular Junctions ◽  
Adherens Junction Proteins ◽  
Junction Proteins

scholarly journals β-Catenin N- and C-terminal Tails Modulate the Coordinated Binding of Adherens Junction Proteins to β-Catenin

2002 ◽  
Vol 277 (35) ◽  
pp. 31541-31550 ◽  
Author(s):  
Julio Castaño ◽  
Imma Raurell ◽  
José A. Piedra ◽  
Susana Miravet ◽  
Mireia Duñach ◽  
...  
Keyword(s):  
Adherens Junction ◽  
Adherens Junction Proteins ◽  
Junction Proteins
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