scholarly journals Epithelial cell-cell contacts regulate SRF-mediated transcription via Rac-actin-MAL signalling

2008 ◽  
Vol 121 (7) ◽  
pp. 1025-1035 ◽  
Author(s):  
S. Busche ◽  
A. Descot ◽  
S. Julien ◽  
H. Genth ◽  
G. Posern
Keyword(s):  
Epithelial Cell ◽  
Cell Contacts ◽  
Cell Cell

scholarly journals A molecular mechanism directly linking E-cadherin adhesion to initiation of epithelial cell surface polarity

2007 ◽  
Vol 178 (2) ◽  
pp. 323-335 ◽  
Author(s):  
Lene N. Nejsum ◽  
W. James Nelson
Keyword(s):  
Cell Adhesion ◽  
Epithelial Cell ◽  
Cell Surface ◽  
Basolateral Membrane ◽  
Surface Polarity ◽  
Cell Contacts ◽  
Protein Receptors ◽  
Epithelial Cell Surface ◽  
E Cadherin ◽  
Cell Cell

Mechanisms involved in maintaining plasma membrane domains in fully polarized epithelial cells are known, but when and how directed protein sorting and trafficking occur to initiate cell surface polarity are not. We tested whether establishment of the basolateral membrane domain and E-cadherin–mediated epithelial cell–cell adhesion are mechanistically linked. We show that the basolateral membrane aquaporin (AQP)-3, but not the equivalent apical membrane AQP5, is delivered in post-Golgi structures directly to forming cell–cell contacts where it co-accumulates precisely with E-cadherin. Functional disruption of individual components of a putative lateral targeting patch (e.g., microtubules, the exocyst, and soluble N-ethylmaleimide–sensitive factor attachment protein receptors) did not inhibit cell–cell adhesion or colocalization of the other components with E-cadherin, but each blocked AQP3 delivery to forming cell–cell contacts. Thus, components of the lateral targeting patch localize independently of each other to cell–cell contacts but collectively function as a holocomplex to specify basolateral vesicle delivery to nascent cell–cell contacts and immediately initiate cell surface polarity.

scholarly journals Anchorage of Microtubule Minus Ends to Adherens Junctions Regulates Epithelial Cell-Cell Contacts

Cell ◽  
2008 ◽  
Vol 135 (5) ◽  
pp. 948-959 ◽  
Author(s):  
Wenxiang Meng ◽  
Yoshimi Mushika ◽  
Tetsuo Ichii ◽  
Masatoshi Takeichi
Keyword(s):  
Epithelial Cell ◽  
Adherens Junctions ◽  
Cell Contacts ◽  
Cell Cell

scholarly journals Distinct Rho GTPase Activities Regulate Epithelial Cell Localization of the Adhesion Molecule CEACAM1: Involvement of the CEACAM1 Transmembrane Domain

2003 ◽  
Vol 23 (20) ◽  
pp. 7291-7304 ◽  
Author(s):  
Bénédicte Fournès ◽  
Jennifer Farrah ◽  
Melanie Olson ◽  
Nathalie Lamarche-Vane ◽  
Nicole Beauchemin
Keyword(s):  
Epithelial Cell ◽  
Epithelial Cells ◽  
Rho Gtpases ◽  
Rho Gtpase ◽  
Transmembrane Domain ◽  
Rho Kinase ◽  
Cell Contacts ◽  
Cell Localization ◽  
Downstream Effector ◽  
Cell Cell

ABSTRACT CEACAM1 is an intercellular adhesion glycoprotein. As CEACAM1 plays an important role in epithelial cell signaling and functions, we have examined its localization in epithelial cells. We have observed that distribution at cell contacts is not always seen in these cells, suggesting that CEACAM1 localization might be regulated. In Swiss 3T3 cells, the targeting of CEACAM1 at cell-cell boundaries is regulated by the Rho GTPases. In the present study, we have used the MDCK epithelial cells to characterize the effects of the Rho GTPases and their effectors on CEACAM1 intercellular targeting. Activated Cdc42 and Rac1 or their downstream effector PAK1 targeted CEACAM1 to sites of cell-cell contacts. On the other hand, neither activated RhoA nor activated Rho kinase directed CEACAM1 to cell boundaries, resulting in a condensed distribution of CEACAM1 at the cell surface. Interestingly, inhibition of this pathway resulted in CEACAM1 intercellular localization suggesting that a tightly regulated balance of Rho GTPase activities is necessary to target CEACAM1 at cell-cell boundaries. In addition, using CEACAM1 mutants and chimeric fusion constructs containing domains of the colony-stimulating factor receptor, we have shown that the transmembrane domain of CEACAM1 is responsible for the Cdc42-induced targeting at cell-cell contacts.

scholarly journals Plasticity in epithelial cell phenotype: modulation by expression of different cadherin cell adhesion molecules.

1995 ◽  
Vol 129 (2) ◽  
pp. 507-519 ◽  
Author(s):  
J A Marrs ◽  
C Andersson-Fisone ◽  
M C Jeong ◽  
L Cohen-Gould ◽  
C Zurzolo ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Epithelial Cell ◽  
Apical Membrane ◽  
Retinal Pigment ◽  
Cell Phenotype ◽  
Cell Contacts ◽  
Membrane Cytoskeleton ◽  
E Cadherin ◽  
Cell Cell

A primary function of cadherins is to regulate cell adhesion. Here, we demonstrate a broader function of cadherins in the differentiation of specialized epithelial cell phenotypes. In situ, the rat retinal pigment epithelium (RPE) forms cell-cell contacts within its monolayer, and at the apical membrane with the neural retina; Na+, K(+)-ATPase and the membrane cytoskeleton are restricted to the apical membrane. In vitro, RPE cells (RPE-J cell line) express an endogenous cadherin, form adherens junctions and a tight monolayer, but Na+,K(+)-ATPase is localized to both apical and basal-lateral membranes. Expression of E-cadherin in RPE-J cells results in restriction and accumulation of both Na+,K(+)-ATPase and the membrane cytoskeleton at the lateral membrane; these changes correlate with the synthesis of a different ankyrin isoform. In contrast to both RPE in situ and RPE-J cells that do not form desmosomes, E-cadherin expression in RPE-J cells induces accumulation of desmoglein mRNA, and assembly of desmosome-keratin complexes at cell-cell contacts. These results demonstrate that cadherins directly affect epithelial cell phenotype by remodeling the distributions of constitutively expressed proteins and by induced accumulation of specific proteins, which together lead to the generation of structurally and functionally distinct epithelial cell types.

scholarly journals The Catalytic Activity of the Src Family Kinases Is Required to Disrupt Cadherin-dependent Cell–Cell Contacts

2000 ◽  
Vol 11 (1) ◽  
pp. 51-64 ◽  
Author(s):  
Dewi W. Owens ◽  
Gordon W. McLean ◽  
Anne W. Wyke ◽  
Christos Paraskeva ◽  
E. Kenneth Parkinson ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Epithelial Cell ◽  
Kinase Inhibitor ◽  
Human Keratinocytes ◽  
Src Family Kinases ◽  
Cell Contact ◽  
Cell Contacts ◽  
Intercellular Contacts ◽  
Cell Cell

Despite the importance of epithelial cell contacts in determining cell behavior, we still lack a detailed understanding of the assembly and disassembly of intercellular contacts. Here we examined the role of the catalytic activity of the Src family kinases at epithelial cell contacts in vitro. Like E- and P-cadherin, Ca2+ treatment of normal and tumor-derived human keratinocytes resulted in c-Yes (and c-Src and Fyn), as well as their putative substrate p120CTN, being recruited to cell–cell contacts. A tyrosine kinase inhibitor with selectivity against the Src family kinases, PD162531, and a dominant-inhibitory c-Src protein that interferes with the catalytic function of the endogenous Src kinases induced cell–cell contact and E-cadherin redistribution, even in low Ca2+, which does not normally support stable cell–cell adhesion. Time-lapse microscopy demonstrated that Src kinase inhibition induced stabilization of transiently formed intercellular contacts in low Ca2+. Furthermore, a combination of E- and P-cadherin-specific antibodies suppressed cell–cell contact, indicating cadherin involvement. As a consequence of contact stabilization, normal cells were unable to dissociate from an epithelial sheet formed at high density and repair a wound in vitro, although individual cells were still motile. Thus, cadherin-dependent contacts can be stabilized both by high Ca2+ and by inhibiting Src activity in low (0.03 mM) Ca2+ in vitro.

scholarly journals Scribble is required for normal epithelial cell–cell contacts and lumen morphogenesis in the mammalian lung

2013 ◽  
Vol 373 (2) ◽  
pp. 267-280 ◽  
Author(s):  
Laura L. Yates ◽  
Carsten Schnatwinkel ◽  
Lee Hazelwood ◽  
Lauren Chessum ◽  
Anju Paudyal ◽  
...  
Keyword(s):  
Epithelial Cell ◽  
Normal Epithelial Cell ◽  
Cell Contacts ◽  
Mammalian Lung ◽  
Cell Cell

scholarly journals Proteasome-mediated Degradation of Rac1-GTP during Epithelial Cell Scattering

2006 ◽  
Vol 17 (5) ◽  
pp. 2236-2242 ◽  
Author(s):  
Emma A. Lynch ◽  
Jennifer Stall ◽  
Gudila Schmidt ◽  
Philippe Chavrier ◽  
Crislyn D'Souza-Schorey
Keyword(s):  
Epithelial Cell ◽  
Actin Polymerization ◽  
Actin Dynamics ◽  
Cell Contacts ◽  
Rho Family Gtpases ◽  
Cell Scattering ◽  
Rho Family ◽  
Powerful Mechanism ◽  
Sustained Activation ◽  
Cell Cell

Epithelial cells disassemble their adherens junctions and “scatter” during processes such as tumor cell invasion as well as some stages of embryonic development. Control of actin polymerization is a powerful mechanism for regulating the strength of cell–cell adhesion. In this regard, studies have shown that sustained activation of Rac1, a well-known regulator of actin dynamics, results in the accumulation of polymerized actin at cell–cell contacts in epithelia and an increase in E-cadherin–mediated adhesion. Here we show that active Rac1 is ubiquitinated and subject to proteasome-mediated degradation during the early stages of epithelial cell scattering. These findings delineate a mechanism for the down-regulation of Rac1 in the disassembly of epithelial cell–cell contacts and support the emerging theme that UPS-mediated degradation of the Rho family GTPases may serve as an efficient mechanism for GTPase deactivation in the sustained presence of Dbl-exchange factors.

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