scholarly journals Propagating actomyosin-generated force to intercellular junction

2017 ◽  
Author(s):  
Vivian W. Tang
Keyword(s):  
Cell Adhesion ◽  
Epithelial Cells ◽  
Intercellular Junction ◽  
Junctional Complex ◽  
Lateral Membrane ◽  
Tension Response ◽  
Actomyosin Contractility ◽  
Adhesion Complex ◽  
Cell Interface ◽  
Cell Cell

AbstractActomyosin II contractility in epithelial cells plays an essential role in tension-dependent adhesion strengthening. One key unsettling question is how cellular contraction transmits force to nascent cell-cell adhesion when there is no stable attachment between the nascent adhesion complex and actin filament. Here, we showed that application of intercellular tension induces myosin 1c accumulation at the lateral membrane between epithelial cells. We hypothesized that the accumulation of myosin 1c at the cell-cell interface allows coupling of actomyosin contractility to the generation of intercellular tension, thus is essential for tension-induced junction maturation. We showed that myosin 1c KD compromises a-actinin-4 recruitment to cell-cell adhesion during normal junction maturation driven by endogenous actomyosin contractility. However, application of cyclic tension to intercellular junction from outside of the cells rescued tension-dependent a-actinin-4 accumulation, suggesting that myosin-1c KD did not compromise the tension response or disrupt the overall integrity of the junctional complex. Our study identifies myosin-1c as a novel tension-sensitive protein on the lateral membrane and underscores a non-junctional contribution to adhesion strengthening at the epithelial cell-cell adhesion interface.

scholarly journals Biogenesis of Polarized Epithelial Cells During Kidney Development In Situ: Roles of E-Cadherin–mediated Cell–Cell Adhesion and Membrane Cytoskeleton Organization

1998 ◽  
Vol 9 (11) ◽  
pp. 3161-3177 ◽  
Author(s):  
Peter A. Piepenhagen ◽  
W. James Nelson
Keyword(s):  
Cell Adhesion ◽  
Epithelial Cells ◽  
Kidney Development ◽  
Lateral Membrane ◽  
Membrane Cytoskeleton ◽  
Triton X ◽  
E Cadherin ◽  
Cell Cell

Organization of proteins into structurally and functionally distinct plasma membrane domains is an essential characteristic of polarized epithelial cells. Based on studies with cultured kidney cells, we have hypothesized that a mechanism for restricting Na/K-ATPase to the basal-lateral membrane involves E-cadherin–mediated cell–cell adhesion and integration of Na/K-ATPase into the Triton X-100–insoluble ankyrin- and spectrin-based membrane cytoskeleton. In this study, we examined the relevance of these in vitro observations to the generation of epithelial cell polarity in vivo during mouse kidney development. Using differential detergent extraction, immunoblotting, and immunofluorescence histochemistry, we demonstrate the following. First, expression of the 220-kDa splice variant of ankyrin-3 correlates with the development of resistance to Triton X-100 extraction for Na/K-ATPase, E-cadherin, and catenins and precedes maximal accumulation of Na/K-ATPase. Second, expression of the 190-kDa slice variant of ankyrin-3 correlates with maximal accumulation of Na/K-ATPase. Third, Na/K-ATPase, ankyrin-3, and fodrin specifically colocalize at the basal-lateral plasma membrane of all epithelial cells in which they are expressed and during all stages of nephrogenesis. Fourth, the relative immunofluorescence staining intensities of Na/K-ATPase, ankyrin-3, and fodrin become more similar during development until they are essentially identical in adult kidney. Thus, renal epithelial cells in vivo regulate the accumulation of E-cadherin–mediated adherens junctions, the membrane cytoskeleton, and Na/K-ATPase through sequential protein expression and assembly on the basal-lateral membrane. These results are consistent with a mechanism in which generation and maintenance of polarized distributions of these proteins in vivo and in vitro involve cell–cell adhesion, assembly of the membrane cytoskeleton complex, and concomitant integration and retention of Na/K-ATPase in this complex.

scholarly journals Cell–cell adhesion interface: orthogonal and parallel forces from contraction, protrusion, and retraction

F1000Research ◽  
2018 ◽  
Vol 7 ◽  
pp. 1544 ◽  
Author(s):  
Vivian W. Tang
Keyword(s):  
Cell Adhesion ◽  
Epithelial Cell ◽  
Mechanical Force ◽  
Cell Behavior ◽  
Cellular Forces ◽  
The Relationship ◽  
Cell Interface ◽  
Lateral Cell ◽  
Strength Of Adhesion ◽  
Cell Cell

The epithelial lateral membrane plays a central role in the integration of intercellular signals and, by doing so, is a principal determinant in the emerging properties of epithelial tissues. Mechanical force, when applied to the lateral cell–cell interface, can modulate the strength of adhesion and influence intercellular dynamics. Yet the relationship between mechanical force and epithelial cell behavior is complex and not completely understood. This commentary aims to provide an investigative look at the usage of cellular forces at the epithelial cell–cell adhesion interface.

Expression and role of E- and P-cadherin adhesion molecules in embryonic histogenesis. I. Lung epithelial morphogenesis

Development ◽  
1989 ◽  
Vol 105 (2) ◽  
pp. 263-270 ◽  
Author(s):  
Y. Hirai ◽  
A. Nose ◽  
S. Kobayashi ◽  
M. Takeichi
Keyword(s):  
Monoclonal Antibody ◽  
Cell Adhesion ◽  
Epithelial Cells ◽  
Adhesion Molecules ◽  
Lung Epithelial Cells ◽  
Early Developmental Stage ◽  
Subtle Effect ◽  
Lung Epithelial ◽  
Cell Cell

The role of Ca2+-dependent cell-cell adhesion molecules, E- and P-cadherins, in the histogenesis of mouse embryonic lung was studied. All epithelial cells of the lung express both E- and P-cadherin at the early developmental stage. P-cadherin, however, gradually disappears during development, initially from the main bronchi and eventually from all epithelial cells. When a monoclonal antibody to E-cadherin (ECCD-1) was added to monolayer cultures of lung epithelial cells, it induced a partial disruption of their cell-cell adhesion, while a monoclonal antibody to P-cadherin (PCD-1) showed a subtle effect. A mixture of the two antibodies, however, displayed a synergistic effect. We then tested the effect of the antibodies on the morphogenesis of lung primordia using an organ culture system. In control media, the explants formed typical bronchial trees. In the presence of ECCD-1, the explants grew up at the same rate as in the control, but their morphogenesis was affected. The control explants formed round epithelial lobules with an open luminal space at the tips of the bronchial trees, whereas the lobules of explants incubated with ECCD-1 tended to be flat and devoid of the luminal space. PCD-1 showed a similar but very small effect. A mixture of the two antibodies, however, showed a stronger effect: the branching of epithelia was partially suppressed and the arrangement of epithelial cells was distorted in many places. These results suggest that E- and P-cadherin have a synergistic role in the organization of epithelial cells in lung morphogenesis.

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.

Characterization of a Novel Human IgG Antibody Reactive with a Ca2+-Sensitive Cell-Cell Adhesion Epitope of PtK2 Epithelial Cells

Autoimmunity ◽  
1995 ◽  
Vol 20 (4) ◽  
pp. 237-245 ◽  
Author(s):  
Denis Girard ◽  
Jean-Luc Senécal
Keyword(s):  
Cell Adhesion ◽  
Epithelial Cells ◽  
Sensitive Cell ◽  
Igg Antibody ◽  
Human Igg ◽  
Cell Cell

scholarly journals Sec6/8 Complex Is Recruited to Cell–Cell Contacts and Specifies Transport Vesicle Delivery to the Basal-Lateral Membrane in Epithelial Cells

Cell ◽  
1998 ◽  
Vol 93 (5) ◽  
pp. 731-740 ◽  
Author(s):  
Kent K Grindstaff ◽  
Charles Yeaman ◽  
Niroshana Anandasabapathy ◽  
Shu-Chan Hsu ◽  
Enrique Rodriguez-Boulan ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Cell Contacts ◽  
Lateral Membrane ◽  
Transport Vesicle ◽  
Cell Cell

scholarly journals c-Yes regulates cell adhesion at the apical ectoplasmic specialization-blood-testis barrier axis via its effects on protein recruitment and distribution

2013 ◽  
Vol 304 (2) ◽  
pp. E145-E159 ◽  
Author(s):  
Xiang Xiao ◽  
Dolores D. Mruk ◽  
C. Yan Cheng
Keyword(s):  
Cell Adhesion ◽  
Sertoli Cell ◽  
Germ Cells ◽  
Early Stage ◽  
Seminiferous Epithelium ◽  
Permeability Barrier ◽  
Cell Interface ◽  
Ectoplasmic Specialization ◽  
Cell Cell ◽  
Blood Testis Barrier

During spermatogenesis, extensive restructuring takes place at the cell-cell interface since developing germ cells migrate progressively from the basal to the adluminal compartment of the seminiferous epithelium. Since germ cells per se are not motile cells, their movement relies almost exclusively on the Sertoli cell. Nonetheless, extensive exchanges in signaling take place between these cells in the seminiferous epithelium. c-Yes, a nonreceptor protein tyrosine kinase belonging to the Src family kinases (SFKs) and a crucial signaling protein, was recently shown to be upregulated at the Sertoli cell-cell interface at the blood-testis barrier (BTB) at stages VIII–IX of the seminiferous epithelial cycle of spermatogenesis. It was also highly expressed at the Sertoli cell-spermatid interface known as apical ectoplasmic specialization (apical ES) at stage V to early stage VIII of the epithelial cycle during spermiogenesis. Herein, it was shown that the knockdown of c-Yes by RNAi in vitro and in vivo affected both Sertoli cell adhesion at the BTB and spermatid adhesion at the apical ES, causing a disruption of the Sertoli cell tight junction-permeability barrier function, germ cell loss from the seminiferous epithelium, and also a loss of spermatid polarity. These effects were shown to be mediated by changes in distribution and/or localization of adhesion proteins at the BTB (e.g., occludin, N-cadherin) and at the apical ES (e.g., nectin-3) and possibly the result of changes in the underlying actin filaments at the BTB and the apical ES. These findings implicate that c-Yes is a likely target of male contraceptive research.

scholarly journals Purinergic receptor (P2X7) activation reduces cell–cell adhesion between tubular epithelial cells of the proximal kidney

2019 ◽  
Vol 22 ◽  
pp. 102108 ◽  
Author(s):  
Eleftherios Siamantouras ◽  
Gareth W. Price ◽  
Joe A. Potter ◽  
Claire E. Hills ◽  
Paul E. Squires
Keyword(s):  
Cell Adhesion ◽  
Epithelial Cells ◽  
Purinergic Receptor ◽  
Tubular Epithelial Cells ◽  
Cell Cell
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