scholarly journals α3 Integrin of Cell-Cell Contact Mediates Kidney Fibrosis by Integrin-Linked Kinase in Proximal Tubular E-Cadherin Deficient Mice

2016 ◽  
Vol 186 (7) ◽  
pp. 1847-1860 ◽  
Author(s):  
Guoping Zheng ◽  
Jianlin Zhang ◽  
Hong Zhao ◽  
Hailong Wang ◽  
Min Pang ◽  
...  
Keyword(s):  
Cell Contact ◽  
Kidney Fibrosis ◽  
Proximal Tubular ◽  
Integrin Linked Kinase ◽  
Α3 Integrin ◽  
Deficient Mice ◽  
E Cadherin ◽  
Cell Cell

scholarly journals Remodeling the cell surface distribution of membrane proteins during the development of epithelial cell polarity.

1992 ◽  
Vol 116 (4) ◽  
pp. 889-899 ◽  
Author(s):  
D A Wollner ◽  
K A Krzeminski ◽  
W J Nelson
Keyword(s):  
Epithelial Cell ◽  
Membrane Proteins ◽  
Cell Surface ◽  
Mdck Cells ◽  
Apical Cell ◽  
Cell Contact ◽  
Surface Polarity ◽  
Lateral Membrane ◽  
E Cadherin ◽  
Cell Cell

The development of polarized epithelial cells from unpolarized precursor cells follows induction of cell-cell contacts and requires resorting of proteins into different membrane domains. We show that in MDCK cells the distributions of two membrane proteins, Dg-1 and E-cadherin, become restricted to the basal-lateral membrane domain within 8 h of cell-cell contact. During this time, however, 60-80% of newly synthesized Dg-1 and E-cadherin is delivered directly to the forming apical membrane and then rapidly removed, while the remainder is delivered to the basal-lateral membrane and has a longer residence time. Direct delivery of greater than 95% of these proteins from the Golgi complex to the basal-lateral membrane occurs greater than 48 h later. In contrast, we show that two apical proteins are efficiently delivered and restricted to the apical cell surface within 2 h after cell-cell contact. These results provide insight into mechanisms involved in the development of epithelial cell surface polarity, and the establishment of protein sorting pathways in polarized cells.

scholarly journals Changes in E-cadherin rigidity sensing regulate cell adhesion

2017 ◽  
Vol 114 (29) ◽  
pp. E5835-E5844 ◽  
Author(s):  
Caitlin Collins ◽  
Aleksandra K. Denisin ◽  
Beth L. Pruitt ◽  
W. James Nelson
Keyword(s):  
Cell Adhesion ◽  
Signaling Molecules ◽  
Membrane Dynamics ◽  
Cell Contact ◽  
Adhesion Assay ◽  
Cell Periphery ◽  
Actin Organization ◽  
Rigidity Sensing ◽  
E Cadherin ◽  
Cell Cell

Mechanical cues are sensed and transduced by cell adhesion complexes to regulate diverse cell behaviors. Extracellular matrix (ECM) rigidity sensing by integrin adhesions has been well studied, but rigidity sensing by cadherins during cell adhesion is largely unexplored. Using mechanically tunable polyacrylamide (PA) gels functionalized with the extracellular domain of E-cadherin (Ecad-Fc), we showed that E-cadherin–dependent epithelial cell adhesion was sensitive to changes in PA gel elastic modulus that produced striking differences in cell morphology, actin organization, and membrane dynamics. Traction force microscopy (TFM) revealed that cells produced the greatest tractions at the cell periphery, where distinct types of actin-based membrane protrusions formed. Cells responded to substrate rigidity by reorganizing the distribution and size of high-traction-stress regions at the cell periphery. Differences in adhesion and protrusion dynamics were mediated by balancing the activities of specific signaling molecules. Cell adhesion to a 30-kPa Ecad-Fc PA gel required Cdc42- and formin-dependent filopodia formation, whereas adhesion to a 60-kPa Ecad-Fc PA gel induced Arp2/3-dependent lamellipodial protrusions. A quantitative 3D cell–cell adhesion assay and live cell imaging of cell–cell contact formation revealed that inhibition of Cdc42, formin, and Arp2/3 activities blocked the initiation, but not the maintenance of established cell–cell adhesions. These results indicate that the same signaling molecules activated by E-cadherin rigidity sensing on PA gels contribute to actin organization and membrane dynamics during cell–cell adhesion. We hypothesize that a transition in the stiffness of E-cadherin homotypic interactions regulates actin and membrane dynamics during initial stages of cell–cell adhesion.

scholarly journals RNAi-Mediated Knock-Down of Arylamine N-acetyltransferase-1 Expression Induces E-cadherin Up-Regulation and Cell-Cell Contact Growth Inhibition

PLoS ONE ◽  
2011 ◽  
Vol 6 (2) ◽  
pp. e17031 ◽  
Author(s):  
Jacky M. Tiang ◽  
Neville J. Butcher ◽  
Carleen Cullinane ◽  
Patrick O. Humbert ◽  
Rodney F. Minchin
Keyword(s):  
Growth Inhibition ◽  
Cell Contact ◽  
Knock Down ◽  
E Cadherin ◽  
Cell Cell

E-cadherin mediated cell adhesion recruits SAP97 into the cortical cytoskeleton

1998 ◽  
Vol 111 (8) ◽  
pp. 1071-1080 ◽  
Author(s):  
S.M. Reuver ◽  
C.C. Garner
Keyword(s):  
Cell Adhesion ◽  
Model Systems ◽  
Molecular Organization ◽  
Cell Contact ◽  
Adhesion Sites ◽  
Associated Proteins ◽  
Adhesion Complex ◽  
Cortical Cytoskeleton ◽  
E Cadherin ◽  
Cell Cell

Members of the SAP family of synapse-associated proteins have recently emerged as central players in the molecular organization of synapses. In this study, we have examined the mechanism that localizes one member, SAP97, to sites of cell-cell contact. Utilizing epithelial CACO-2 cells and fibroblast L-cells as model systems, we demonstrate that SAP97 is associated with the submembranous cortical cytoskeleton at cell-cell adhesion sites. Furthermore, we show that its localization into this structure is triggered by E-cadherin. Although SAP97 can be found in an E-cadherin/catenin adhesion complex, this interaction seems to be mediated by the attachment of SAP97 to the cortical cytoskeleton. Our results are consistent with a model in which SAP97 is recruited to sites of cell-cell contact via an E-cadherin induced assembly of the cortical cytoskeleton.

scholarly journals p120-Catenin Is a Key Component of the Cadherin–γ-Secretase Supercomplex

2008 ◽  
Vol 19 (10) ◽  
pp. 4042-4050 ◽  
Author(s):  
Alexi Kiss ◽  
Regina B. Troyanovsky ◽  
Sergey M. Troyanovsky
Keyword(s):  
Proteolytic Activity ◽  
Cell Contact ◽  
Compelling Evidence ◽  
P120 Catenin ◽  
Low Level ◽  
High Affinity ◽  
Affinity Interaction ◽  
E Cadherin ◽  
Cell Cell

In this work, we show several previously unknown features of p120-catenin in a cadherin–catenin complex that are critical for our understanding of cadherin-based adhesion and signaling. We show that in human epithelial A-431 cells, nearly all p120 molecules engage in high-affinity interaction with E-cadherin–catenin complexes located at the cellular surface. p120 is positioned in proximity to α-catenin in the complex with cadherin. These findings suggest a functional cooperation between p120 and α-catenin in cadherin-based adhesion. A low level of cadherin-free p120 molecules, in contrast, could facilitate p120-dependent signaling. Finally, we present compelling evidence that p120 is a key linker cementing the E-cadherin–catenin complex with the transmembrane protease γ-secretase. The cell–cell contact location of this supercomplex makes it an important candidate for conducting different signals that rely on γ-secretase proteolytic activity.

scholarly journals Abrogation of E-Cadherin-Mediated Cell-Cell Contact in Mouse Embryonic Stem Cells Results in Reversible LIF-Independent Self-Renewal

Stem Cells ◽  
2009 ◽  
Vol 27 (9) ◽  
pp. 2069-2080 ◽  
Author(s):  
Francesca Soncin ◽  
Lisa Mohamet ◽  
Dominik Eckardt ◽  
Sarah Ritson ◽  
Angela M. Eastham ◽  
...  
Keyword(s):  
Stem Cells ◽  
Embryonic Stem Cells ◽  
Embryonic Stem ◽  
Mouse Embryonic Stem Cells ◽  
Cell Contact ◽  
Self Renewal ◽  
E Cadherin ◽  
Cell Cell

scholarly journals The formation of ordered nanoclusters controls cadherin anchoring to actin and cell–cell contact fluidity

2015 ◽  
Vol 210 (2) ◽  
pp. 333-346 ◽  
Author(s):  
Pierre-Olivier Strale ◽  
Laurence Duchesne ◽  
Grégoire Peyret ◽  
Lorraine Montel ◽  
Thao Nguyen ◽  
...  
Keyword(s):  
Adherens Junction ◽  
Intercellular Junctions ◽  
Cell Contact ◽  
Collective Cell Migration ◽  
Contact Stability ◽  
Junction Formation ◽  
Mediate Cell ◽  
The Stability ◽  
E Cadherin ◽  
Cell Cell

Oligomerization of cadherins could provide the stability to ensure tissue cohesion. Cadherins mediate cell–cell adhesion by forming trans-interactions. They form cis-interactions whose role could be essential to stabilize intercellular junctions by shifting cadherin clusters from a fluid to an ordered phase. However, no evidence has been provided so far for cadherin oligomerization in cellulo and for its impact on cell–cell contact stability. Visualizing single cadherins within cell membrane at a nanometric resolution, we show that E-cadherins arrange in ordered clusters, providing the first demonstration of the existence of oligomeric cadherins at cell–cell contacts. Studying the consequences of the disruption of the cis-interface, we show that it is not essential for adherens junction formation. Its disruption, however, increased the mobility of junctional E-cadherin. This destabilization strongly affected E-cadherin anchoring to actin and cell–cell rearrangement during collective cell migration, indicating that the formation of oligomeric clusters controls the anchoring of cadherin to actin and cell–cell contact fluidity.

The Impact of Cell-Cell Contact, E-Cadherin and EGF Receptor on the Cellular Radiosensitivity of A431 Cancer Cells

2012 ◽  
Vol 178 (3) ◽  
pp. 224-233 ◽  
Author(s):  
Ercole Mazzeo ◽  
Stephanie Hehlgans ◽  
Vincenzo Valentini ◽  
Michael Baumann ◽  
Nils Cordes
Keyword(s):  
Cancer Cells ◽  
Egf Receptor ◽  
Cell Contact ◽  
Cellular Radiosensitivity ◽  
The Impact ◽  
E Cadherin ◽  
Cell Cell

Overexpression of the integrin-linked kinase mesenchymally transforms mammary epithelial cells

2001 ◽  
Vol 114 (6) ◽  
pp. 1125-1136 ◽  
Author(s):  
A. Somasiri ◽  
A. Howarth ◽  
D. Goswami ◽  
S. Dedhar ◽  
C.D. Roskelley
Keyword(s):  
Epithelial Cell ◽  
Epithelial Cells ◽  
Mammary Epithelial Cell ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Cell Morphogenesis ◽  
Wild Type ◽  
Integrin Linked Kinase ◽  
E Cadherin ◽  
Cell Cell

Signals generated by the interaction of (β)1 integrins with laminin in the basement membrane contribute to mammary epithelial cell morphogenesis and differentiation. The integrin-linked kinase (ILK) is one of the signaling moieties that associates with the cytoplasmic domain of (β)1 integrin subunits with some specificity. Forced expression of a dominant negative, kinase-dead form of ILK subtly altered mouse mammary epithelial cell morphogenesis but it did not prevent differentiative milk protein expression. In contrast, forced overexpression of wild-type ILK strongly inhibited both morphogenesis and differentiation. Overexpression of wild-type ILK also caused the cells to lose the cell-cell adhesion molecule E-cadherin, become invasive, reorganize cortical actin into cytoplasmic stress fibers, and switch from an epithelial cytokeratin to a mesenchymal vimentin intermediate filament phenotype. Forced expression of E-cadherin in the latter mesenchymal cells rescued epithelial cytokeratin expression and it partially restored the ability of the cells to differentiate and undergo morphogenesis. These data demonstrate that ILK, which responds to interactions between cells and the extracellular matrix, induces a mesenchymal transformation in mammary epithelial cells, at least in part, by disrupting cell-cell junctions.

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