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 Role of IQGAP1 in endothelial barrier enhancement caused by OxPAPC

2016 ◽  
Vol 311 (4) ◽  
pp. L800-L809 ◽  
Author(s):  
Yufeng Tian ◽  
Xinyong Tian ◽  
Grzegorz Gawlak ◽  
Nicolene Sarich ◽  
David B. Sacks ◽  
...  
Keyword(s):  
Actin Cytoskeleton ◽  
Actin Polymerization ◽  
Adherens Junctions ◽  
Adherens Junction ◽  
Cell Junctions ◽  
Endothelial Barrier ◽  
Cell Junction ◽  
Protective Effects ◽  
P120 Catenin

Oxidized 1-palmitoyl-2-arachidonoyl- sn-glycero-3-phosphatidylcholine (OxPAPC) attenuates agonist-induced endothelial cell (EC) permeability and increases pulmonary endothelial barrier function via enhancement of both the peripheral actin cytoskeleton and cell junctions mediated by Rac1 and Cdc42 GTPases. This study evaluated the role for the multifunctional Rac1/Cdc42 effector and regulator, IQ domain containing GTPase-activating protein (IQGAP1), as a molecular transducer of the OxPAPC-mediated EC barrier-enhancing signal. IQGAP1 knockdown in endothelial cells by gene-specific small-interfering RNA abolished OxPAPC-induced enlargement of VE-cadherin-positive adherens junctions, suppressed peripheral accumulation of actin polymerization regulators, namely cortactin, neural Wiskott-Aldrich syndrome protein (N-WASP), and actin-related protein 3, and attenuated remodeling of the peripheral actin cytoskeleton. Inhibition of OxPAPC-induced barrier enhancement by IQGAP1 knockdown was due to suppressed Rac1 and Cdc42 activation. Expression of an IQGAP1 truncated mutant showed that the GTPase regulatory domain of IQGAP1 was essential for the OxPAPC-induced membrane localization of cortactin, adherens junction proteins VE-cadherin and p120-catenin, as well as for EC permeability response. IQGAP1 knockdown attenuated the protective effect of OxPAPC against thrombin-induced cell contraction, cell junction disruption, and EC permeability. These results demonstrate for the first time the role of IQGAP1 as a critical transducer of OxPAPC-induced Rac1/Cdc42 signaling to the actin cytoskeleton and adherens junctions, which promotes cortical cytoskeletal remodeling and EC barrier-protective effects of oxidized phospholipids.

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 Role of Adherens Junction Proteins in Differential Herpes Simplex Virus Type 2 Infectivity in Communication-Competent and -Deficient Cell Lines

Intervirology ◽  
2012 ◽  
Vol 55 (6) ◽  
pp. 465-474
Author(s):  
Blair Miezeiewski ◽  
Kerry McShane-Kay ◽  
Richard I. Woodruff ◽  
Gustave K.N. Mbuy ◽  
Maureen T. Knabb
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Cell Lines ◽  
Herpes Simplex Virus Type ◽  
Adherens Junction ◽  
Simplex Virus ◽  
Adherens Junction Proteins ◽  
Junction Proteins

scholarly journals Regulating polarity by directing traffic: Cdc42 prevents adherens junctions from Crumblin' aPart

2008 ◽  
Vol 183 (6) ◽  
pp. 971-974 ◽  
Author(s):  
Mara C. Duncan ◽  
Mark Peifer
Keyword(s):  
Cell Adhesion ◽  
Actin Cytoskeleton ◽  
Cell Polarity ◽  
Adherens Junctions ◽  
Vesicular Trafficking ◽  
Cell Junction ◽  
Par Proteins ◽  
Cell Biol ◽  
Embryonic Morphogenesis ◽  
Junction Proteins

The GTPase Cdc42 was among the original genes identified with roles in cell polarity, and interest in its cellular roles from yeast to humans remains high. Cdc42 is a well-known regulator of the actin cytoskeleton, but also plays important roles in vesicular trafficking. In this issue, Harris and Tepass (Harris, K.P, and U. Tepass. 2008. J. Cell. Biol. 183:1129–1143) provide new insights into how Cdc42 and Par proteins work together to modulate cell adhesion and polarity during embryonic morphogenesis by regulating the traffic of key cell junction proteins.

scholarly journals Golgi-associated cPLA2α Regulates Endothelial Cell–Cell Junction Integrity by Controlling the Trafficking of Transmembrane Junction Proteins

2009 ◽  
Vol 20 (19) ◽  
pp. 4225-4234 ◽  
Author(s):  
Elsa Regan-Klapisz ◽  
Vincent Krouwer ◽  
Miriam Langelaar-Makkinje ◽  
Laxman Nallan ◽  
Michael Gelb ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Intracellular Trafficking ◽  
Adherens Junction ◽  
Cell Junctions ◽  
Cell Junction ◽  
Tight Junction Formation ◽  
Junction Formation ◽  
Junction Proteins ◽  
Cell Cell

In endothelial cells specifically, cPLA2α translocates from the cytoplasm to the Golgi complex in response to cell confluence. Considering the link between confluence and cell–cell junction formation, and the emerging role of cPLA2α in intracellular trafficking, we tested whether Golgi-associated cPLA2α is involved in the trafficking of junction proteins. Here, we show that the redistribution of cPLA2α from the cytoplasm to the Golgi correlates with adherens junction maturation and occurs before tight junction formation. Disruption of adherens junctions using a blocking anti-VE-cadherin antibody reverses the association of cPLA2α with the Golgi. Silencing of cPLA2α and inhibition of cPLA2α enzymatic activity using various inhibitors result in the diminished presence of the transmembrane junction proteins VE-cadherin, occludin, and claudin-5 at cell–cell contacts, and in their accumulation at the Golgi. Altogether, our data support the idea that VE-cadherin triggers the relocation of cPLA2α to the Golgi and that in turn, Golgi-associated cPLA2α regulates the transport of transmembrane junction proteins through or from the Golgi, thereby controlling the integrity of endothelial cell–cell junctions.

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

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 Cross-Talk between Adherens Junctions and Desmosomes Depends on Plakoglobin

1997 ◽  
Vol 136 (4) ◽  
pp. 919-934 ◽  
Author(s):  
Jani E. Lewis ◽  
James K. Wahl ◽  
Kristin M. Sass ◽  
Pamela J. Jensen ◽  
Keith R. Johnson ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Cell Line ◽  
Adherens Junctions ◽  
Adherens Junction ◽  
Epithelial Cell Line ◽  
Cell Contact ◽  
Common Component ◽  
Classical Cadherins ◽  
E Cadherin

Squamous epithelial cells have both adherens junctions and desmosomes. The ability of these cells to organize the desmosomal proteins into a functional structure depends upon their ability first to organize an adherens junction. Since the adherens junction and the desmosome are separate structures with different molecular make up, it is not immediately obvious why formation of an adherens junction is a prerequisite for the formation of a desmosome. The adherens junction is composed of a transmembrane classical cadherin (E-cadherin and/or P-cadherin in squamous epithelial cells) linked to either β-catenin or plakoglobin, which is linked to α-catenin, which is linked to the actin cytoskeleton. The desmosome is composed of transmembrane proteins of the broad cadherin family (desmogleins and desmocollins) that are linked to the intermediate filament cytoskeleton, presumably through plakoglobin and desmoplakin. To begin to study the role of adherens junctions in the assembly of desmosomes, we produced an epithelial cell line that does not express classical cadherins and hence is unable to organize desmosomes, even though it retains the requisite desmosomal components. Transfection of E-cadherin and/or P-cadherin into this cell line did not restore the ability to organize desmosomes; however, overexpression of plakoglobin, along with E-cadherin, did permit desmosome organization. These data suggest that plakoglobin, which is the only known common component to both adherens junctions and desmosomes, must be linked to E-cadherin in the adherens junction before the cell can begin to assemble desmosomal components at regions of cell–cell contact. Although adherens junctions can form in the absence of plakoglobin, making use only of β-catenin, such junctions cannot support the formation of desmosomes. Thus, we speculate that plakoglobin plays a signaling role in desmosome organization.

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