Adherens junctions in theDrosophila embryo: The role of E-cadherin in their establishment and morphogenetic function

BioEssays ◽  
1996 ◽  
Vol 18 (8) ◽  
pp. 609-612 ◽  
Author(s):  
Elisabeth Knust ◽  
Maria Leptin
Keyword(s):  
Adherens Junctions ◽  
E Cadherin

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.

scholarly journals The Interaction of JRAB/MICAL-L2 with Rab8 and Rab13 Coordinates the Assembly of Tight Junctions and Adherens Junctions

2008 ◽  
Vol 19 (3) ◽  
pp. 971-983 ◽  
Author(s):  
Rie Yamamura ◽  
Noriyuki Nishimura ◽  
Hiroyoshi Nakatsuji ◽  
Seiji Arase ◽  
Takuya Sasaki
Keyword(s):  
Plasma Membrane ◽  
Epithelial Cells ◽  
Tight Junctions ◽  
Binding Protein ◽  
Adherens Junctions ◽  
Binding Domain ◽  
Endocytic Recycling ◽  
E Cadherin

The assembly of tight junctions (TJs) and adherens junctions (AJs) is regulated by the transport of integral TJ and AJ proteins to and/or from the plasma membrane (PM) and it is tightly coordinated in epithelial cells. We previously reported that Rab13 and a junctional Rab13-binding protein (JRAB)/molecule interacting with CasL-like 2 (MICAL-L2) mediated the endocytic recycling of an integral TJ protein occludin and the formation of functional TJs. Here, we investigated the role of Rab13 and JRAB/MICAL-L2 in the transport of other integral TJ and AJ proteins claudin-1 and E-cadherin to the PM by using a Ca2+-switch model. Although knockdown of Rab13 specifically suppressed claudin-1 and occludin but not E-cadherin transport, knockdown of JRAB/MICAL-L2 and expression of its Rab13-binding domain (JRAB/MICAL-L2-C) inhibited claudin-1, occludin, and E-cadherin transport. We then identified Rab8 as another JRAB/MICAL-L2-C-binding protein. Knockdown of Rab8 inhibited the Rab13-independent transport of E-cadherin to the PM. Rab8 and Rab13 competed with each other for the binding to JRAB/MICAL-L2 and functionally associated with JRAB/MICAL-L2 at the perinuclear recycling/storage compartments and PM, respectively. These results suggest that the interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the assembly of AJs and TJs.

scholarly journals A Novel Role of Nectins in Inhibition of the E-Cadherin–induced Activation of Rac and Formation of Cell-Cell Adherens Junctions

2004 ◽  
Vol 15 (3) ◽  
pp. 1077-1088 ◽  
Author(s):  
Takashi Hoshino ◽  
Kazuya Shimizu ◽  
Tomoyuki Honda ◽  
Tomomi Kawakatsu ◽  
Taihei Fukuyama ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
G Protein ◽  
Adherens Junctions ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Inhibitory Effect ◽  
Small G Protein ◽  
E Cadherin ◽  
Cell Cell

Nectins are Ca2+-independent immunoglobulin (Ig)-like cell-cell adhesion molecules. The trans-interactions of nectins recruit cadherins to the nectin-based cell-cell adhesion, resulting in formation of cell-cell adherens junctions (AJs) in epithelial cells and fibroblasts. The trans-interaction of E-cadherin induces activation of Rac small G protein, whereas the trans-interactions of nectins induce activation of not only Rac but also Cdc42 small G protein. We showed by the fluorescent resonance energy transfer (FRET) imaging that the trans-interaction of E-cadherin induced dynamic activation and inactivation of Rac, which led to dynamic formation and retraction of lamellipodia. Moreover, we found here that the nectins, which did not trans-interact with other nectins (non–trans-interacting nectins), inhibited the E-cadherin–induced activation of Rac and reduced the velocity of the formation of the E-cadherin-based cell-cell AJs. The inhibitory effect of non–trans-interacting nectins was suppressed by the activation of Cdc42 induced by the trans-interactions of nectins. These results indicate a novel role of nectins in regulation of the E-cadherin–induced activation of Rac and formation of cell-cell AJs.

scholarly journals A Novel Role of E-Cadherin-Based Adherens Junctions in Neoplastic Cell Dissemination

PLoS ONE ◽  
2015 ◽  
Vol 10 (7) ◽  
pp. e0133578 ◽  
Author(s):  
Svetlana N. Rubtsova ◽  
Irina Y. Zhitnyak ◽  
Natalya A. Gloushankova
Keyword(s):  
Adherens Junctions ◽  
Neoplastic Cell ◽  
Cell Dissemination ◽  
E Cadherin

410: Cleavage of E-Cadherin and the Role of an 80KDa Fragment in the Metastatic Progression of Prostate Cancer

2004 ◽  
Vol 171 (4S) ◽  
pp. 108-108
Author(s):  
Rainer Kuefer ◽  
Kathleen Day ◽  
Jonathan Rios-Doria ◽  
Matthias Hofer ◽  
Arul Chinnaiyan ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Metastatic Progression ◽  
E Cadherin

scholarly journals Simultaneous Expression of Caveolin-1 and E-Cadherin in Ovarian Carcinoma Cells Stabilizes Adherens Junctions through Inhibition of src-Related Kinases

2005 ◽  
Vol 167 (5) ◽  
pp. 1411-1427 ◽  
Author(s):  
Silvia Miotti ◽  
Antonella Tomassetti ◽  
Ileana Facetti ◽  
Elena Sanna ◽  
Valeria Berno ◽  
...  
Keyword(s):  
Ovarian Carcinoma ◽  
Adherens Junctions ◽  
Carcinoma Cells ◽  
Caveolin 1 ◽  
Ovarian Carcinoma Cells ◽  
Simultaneous Expression ◽  
E Cadherin

scholarly journals Pivotal role of MUC1 glycosylation by cigarette smoke in modulating disruption of airway adherens junctions in vitro

2014 ◽  
Vol 234 (1) ◽  
pp. 60-73 ◽  
Author(s):  
Lili Zhang ◽  
Marianne Gallup ◽  
Lorna Zlock ◽  
Yu Ting Feeling Chen ◽  
Walter E Finkbeiner ◽  
...  
Keyword(s):  
Cigarette Smoke ◽  
Adherens Junctions ◽  
Pivotal Role
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