scholarly journals Mechanism of recruiting Sec6/8 (exocyst) complex to the apical junctional complex during polarization of epithelial cells

2004 ◽  
Vol 117 (4) ◽  
pp. 559-570 ◽  
Author(s):  
C. Yeaman
Keyword(s):  
Epithelial Cells ◽  
Junctional Complex ◽  
Exocyst Complex ◽  
Apical Junctional Complex

scholarly journals Sorbin and SH3 domain-containing protein 2 (SORBS2) is a component of the acto-myosin ring at the apical junctional complex in epithelial cells

PLoS ONE ◽  
2017 ◽  
Vol 12 (9) ◽  
pp. e0185448 ◽  
Author(s):  
Karin Fredriksson-Lidman ◽  
Christina M. Van Itallie ◽  
Amber J. Tietgens ◽  
James M. Anderson
Keyword(s):  
Epithelial Cells ◽  
Sh3 Domain ◽  
Junctional Complex ◽  
Apical Junctional Complex

Dengue virus enters and exits epithelial cells through both apical and basolateral surfaces and perturbs the apical junctional complex

2018 ◽  
Vol 258 ◽  
pp. 39-49
Author(s):  
Liliana Ramirez ◽  
Abigail Betanzos ◽  
Arturo Raya-Sandino ◽  
Lorenza González-Mariscal ◽  
Rosa M. del Angel
Keyword(s):  
Epithelial Cells ◽  
Dengue Virus ◽  
Junctional Complex ◽  
Apical Junctional Complex

scholarly journals Rho/Rho-associated Kinase-II Signaling Mediates Disassembly of Epithelial Apical Junctions

2007 ◽  
Vol 18 (9) ◽  
pp. 3429-3439 ◽  
Author(s):  
Stanislav N. Samarin ◽  
Andrei I. Ivanov ◽  
Gilles Flatau ◽  
Charles A. Parkos ◽  
Asma Nusrat
Keyword(s):  
Epithelial Cells ◽  
Rho Gtpase ◽  
Critical Role ◽  
Junctional Complex ◽  
Nucleotide Exchange ◽  
Calcium Depletion ◽  
Pharmacological Inhibition ◽  
Apical Junctional Complex ◽  
Apical Junctions

Apical junctional complex (AJC) plays a vital role in regulation of epithelial barrier function. Disassembly of the AJC is observed in diverse physiological and pathological states; however, mechanisms governing this process are not well understood. We previously reported that the AJC disassembly is driven by the formation of apical contractile acto-myosin rings. In the present study, we analyzed the signaling pathways regulating acto-myosin–dependent disruption of AJC by using a model of extracellular calcium depletion. Pharmacological inhibition analysis revealed a critical role of Rho-associated kinase (ROCK) in AJC disassembly in calcium-depleted epithelial cells. Furthermore, small interfering RNA (siRNA)-mediated knockdown of ROCK-II, but not ROCK-I, attenuated the disruption of the AJC. Interestingly, AJC disassembly was not dependent on myosin light chain kinase and myosin phosphatase. Calcium depletion resulted in activation of Rho GTPase and transient colocalization of Rho with internalized AJC proteins. Pharmacological inhibition of Rho prevented AJC disassembly. Additionally, Rho guanine nucleotide exchange factor (GEF)-H1 translocated to contractile F-actin rings after calcium depletion, and siRNA-mediated depletion of GEF-H1 inhibited AJC disassembly. Thus, our findings demonstrate a central role of the GEF-H1/Rho/ROCK-II signaling pathway in the disassembly of AJC in epithelial cells.

scholarly journals Defining interactions and distributions of cadherin and catenin complexes in polarized epithelial cells.

1994 ◽  
Vol 125 (6) ◽  
pp. 1341-1352 ◽  
Author(s):  
I S Näthke ◽  
L Hinck ◽  
J R Swedlow ◽  
J Papkoff ◽  
W J Nelson
Keyword(s):  
Epithelial Cells ◽  
Functional Organization ◽  
Insoluble Fraction ◽  
Junctional Complex ◽  
Beta Catenin ◽  
Lateral Membrane ◽  
Apical Junctional Complex ◽  
Polarized Epithelial Cells ◽  
Triton X ◽  
E Cadherin

The cadherin/catenin complex plays important roles in cell adhesion, signal transduction, as well as the initiation and maintenance of structural and functional organization of cells and tissues. In the preceding study, we showed that the assembly of the cadherin/catenin complex is temporally regulated, and that novel combinations of catenin and cadherin complexes are formed in both Triton X-100-soluble and -insoluble fractions; we proposed a model in which pools of catenins are important in regulating assembly of E-cadherin/catenin and catenin complexes. Here, we sought to determine the spatial distributions of E-cadherin, alpha-catenin, beta-catenin, and plakoglobin, and whether different complexes of these proteins accumulate at steady state in polarized Madin-Darby canine kidney cells. Protein distributions were visualized by wide field, optical sectioning, and double immunofluorescence microscopy, followed by reconstruction of three-dimensional images. In cells that were extracted with Triton X-100 and then fixed (Triton X-100-insoluble fraction), more E-cadherin was concentrated at the apical junction relative to other areas of the lateral membrane. alpha-Catenin and beta-catenin colocalize with E-cadherin at the apical junctional complex. There is some overlap in the distribution of these proteins in the lateral membrane, but there are also areas where the distributions are distinct. Plakoglobin is excluded from the apical junctional complex, and its distribution in the lateral membrane is different from that of E-cadherin. Cells were also fixed and then permeabilized to reveal the total cellular pool of each protein (Triton X-100-soluble and -insoluble fractions). This analysis showed lateral membrane localization of alpha-catenin, beta-catenin, and plakoglobin, and it also revealed that they are distributed throughout the cell. Chemical cross-linking of proteins and analysis with specific antibodies confirmed the presence at steady state of E-cadherin/catenin complexes containing either beta-catenin or plakoglobin, and catenin complexes devoid of E-cadherin. Complexes containing E-cadherin/beta-catenin and E-cadherin/alpha-catenin are present in both the Triton X-100-soluble and -insoluble fractions, but E-cadherin/plakoglobin complexes are not detected in the Triton X-100-insoluble fraction. Taken together, these results show that different complexes of cadherin and catenins accumulate in fully polarized epithelial cells, and that they distribute to different sites. We suggest that cadherin/catenin and catenin complexes at different sites have specialized roles in establishing and maintaining the structural and functional organization of polarized epithelial cells.

scholarly journals α-Catenin-Vinculin Interaction Functions to Organize the Apical Junctional Complex in Epithelial Cells

1998 ◽  
Vol 142 (3) ◽  
pp. 847-857 ◽  
Author(s):  
Mitsuko Watabe-Uchida ◽  
Naoshige Uchida ◽  
Yuzo Imamura ◽  
Akira Nagafuchi ◽  
Kazushi Fujimoto ◽  
...  
Keyword(s):  
Amino Acid ◽  
Epithelial Cells ◽  
Tight Junction ◽  
Colon Carcinoma ◽  
Junctional Complex ◽  
F9 Cells ◽  
Terminal Domain ◽  
Apical Junctional Complex ◽  
Internal Domain

αE-catenin, a cadherin-associated protein, is required for tight junction (TJ) organization, but its role is poorly understood. We transfected an αE-catenin–deficient colon carcinoma line with a series of αE-catenin mutant constructs. The results showed that the amino acid 326–509 domain of this catenin was required to organize TJs, and its COOH-terminal domain was not essential for this process. The 326–509 internal domain was found to bind vinculin. When an NH2-terminal αE-catenin fragment, which is by itself unable to organize the TJ, was fused with the vinculin tail, this chimeric molecule could induce TJ assembly in the αE-catenin–deficient cells. In vinculin-null F9 cells, their apical junctional organization was impaired, and this phenotype was rescued by reexpression of vinculin. These results indicate that the αE-catenin-vinculin interaction plays a role in the assembly of the apical junctional complex in epithelia.

Expression and localisation of apical junctional complex proteins in lens epithelial cells

2008 ◽  
Vol 87 (1) ◽  
pp. 64-70 ◽  
Author(s):  
Yuki Sugiyama ◽  
Alan R. Prescott ◽  
Frederique M.D. Tholozan ◽  
Shigeo Ohno ◽  
Roy A. Quinlan
Keyword(s):  
Epithelial Cells ◽  
Lens Epithelial Cells ◽  
Junctional Complex ◽  
Apical Junctional Complex

scholarly journals Endocytosis and Recycling of Tight Junction Proteins in Inflammation

2010 ◽  
Vol 2010 ◽  
pp. 1-6 ◽  
Author(s):  
Markus Utech ◽  
Rudolf Mennigen ◽  
Matthias Bruewer
Keyword(s):  
Epithelial Cells ◽  
Intestinal Epithelial Cells ◽  
Junctional Complex ◽  
Intestinal Epithelial ◽  
Tight Junction Proteins ◽  
Critical Function ◽  
Recycling Endosomes ◽  
Inflammatory Conditions ◽  
Apical Junctional Complex ◽  
Junction Proteins

A critical function of the epithelial lining is to form a barrier that separates luminal contents from the underlying interstitium. This barrier function is primarily regulated by the apical junctional complex (AJC) consisting of tight junctions (TJs) and adherens junctions (AJs) and is compromised under inflammatory conditions. In intestinal epithelial cells, proinflammatory cytokines, for example, interferon-gamma (IFN-γ), induce internalization of TJ proteins by endocytosis. Endocytosed TJ proteins are passed into early and recycling endosomes, suggesting the involvement of recycling of internalized TJ proteins. This review summarizes mechanisms by which TJ proteins under inflammatory conditions are internalized in intestinal epithelial cells and point out comparable mechanism in nonintestinal epithelial cells.

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