ZO-1 Knockout by TALEN-Mediated Gene Targeting in MDCK Cells: Involvement of ZO-1 in the Regulation of Cytoskeleton and Cell Shape

Tokuda, Shinsaku; Higashi, Tomohito; Furuse, Mikio

doi:10.1371/journal.pone.0104994

Cited by 82 publications

(113 citation statements)

References 40 publications

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“…The cell-cell contacts showed a similar jagged shape, and protruded signals of TJ proteins and bleb formation were not observed under the ‘apical hyposmotic’ condition (Fig 9B and 9C and S8 Fig). We also quantified the degree of zigzag in cell-cell contacts (zigzag index) in a similar manner as described previously [25]. The zigzag index was significantly decreased by the apical hyposmolality in wild-type MDCK II cells, and the decrease of the zigzag index by the apical hyposmolality was not observed in claudin-2 knockout clones (Fig 9G).…”

Section: Resultsmentioning

confidence: 81%

“…Quantification of the degree of zigzag in cell-cell contacts was performed as described previously [25]. In brief, the stacked confocal images of ZO-1 staining at the level of tight junctions were acquired and saved as TIFF files.…”

Section: Methodsmentioning

confidence: 99%

“…Time-lapse imaging was performed as described previously [25]. In brief, MDCK II cells expressing Venus-claudin-2 or Venus-Lifeact were cultured on the reverse side of Transwell filter inserts for 6 days.…”

Section: Methodsmentioning

confidence: 99%

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Effects of Osmolality on Paracellular Transport in MDCK II Cells

2016

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Epithelia separate apical and basal compartments, and movement of substances via the paracellular pathway is regulated by tight junctions. Claudins are major constituents of tight junctions and involved in the regulation of tight junction permeability. On the other hand, the osmolality in the extracellular environment fluctuates in association with life activity. However, effects of osmotic changes on the permeaibility of claudins are poorly understood. Therefore, we investigated the effects of osmotic changes on the paracellular transport in MDCK II cells. Interestingly, apical hyposmolality decreased cation selectivity in the paracellular pathway gradually with time, and the elimination of the osmotic gradient promptly restored the cation selectivity. Apical hyposmolality also induced bleb formation at cell-cell contacts and changed the shape of cell-cell contacts from a jagged pattern to a slightly linear pattern. In claudin-2 knockout MDCK II cells, the decrease of cation selectivity, the bleb formation, nor the changes in the shape of cell-cell contacts was observed under the apical hyposmolality. Our findings in this study indicate that osmotic gradient between apical and basal sides is involved in the acute regulation of the cation selective property of claudin-2 channels.

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Section: Resultsmentioning

confidence: 81%

Section: Methodsmentioning

confidence: 99%

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Effects of Osmolality on Paracellular Transport in MDCK II Cells

2016

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“…Transfection of ZO‐1 or ZO‐2 restored junctional integration of myosin‐2 and the establishment of a normal AJ through a mechanism that involved the activation of RhoA and its downstream kinase ROCK . Instead, in MDCK cells lacking ZO‐1 and ZO‐2, the actomyosin bundles at the AJ were highly organized and closely associated with the plasma membrane, while the cells lost their normal linear appearance and acquired a trapezoidal shape, which had also been observed in MDCK ZO‐1 KD and ZO‐1 KO cells . In the latter, the excessive re‐expression of ZO‐1 induced an intensive zigzag cell–cell junction shape.…”

Section: Zo‐2 Functionmentioning

confidence: 85%

ZO‐2, a tight junction protein involved in gene expression, proliferation, apoptosis, and cell size regulation

González‐Mariscal

Miranda

Raya‐Sandino

et al. 2017

Annals of the New York Academy of Sciences

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ZO-2 is a peripheral tight junction protein that belongs to the membrane-associated guanylate kinase protein family. Here, we explain the modular and supramodular organization of ZO-2 that allows it to interact with a wide variety of molecules, including cell-cell adhesion proteins, cytoskeletal components, and nuclear factors. We also describe how ZO proteins evolved through metazoan evolution and analyze the intracellular traffic of ZO-2, as well as the roles played by ZO-2 at the plasma membrane and nucleus that translate into the regulation of proliferation, cell size, and apoptosis. In addition, we focus on the impact of ZO-2 expression on male fertility and on maladies like cancer, cholestasis, and hearing loss.

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“…They interact with JAMs which are expressed on leukocytes and localize on epithelial or endothelial cells functioning in cell-to-cell interaction [97]. JAM has two major roles: the first one is mediating inflammatory reaction between the leukocyte and endothelium, the second one is regulating cell polarity [92]. ZO-1 contains three PDZ domains, one Src homology (SH3), and one guanylate kinase-like (GUK) domain and they make the connection with JAM-A PDZ domain-dependently in epithelial cells and directly associates with membrane and cytosolic proteins such as occludin, claudins, ZO-2 ( Fig.…”

Section: Pdz Domainsmentioning

confidence: 99%

PDZ Domain-containing Proteins at Autotypic Junctions in Myelinating Schwann Cells

Han¹,

Park²,

Hong³

et al. 2015

Journal of Life Science

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A type of cell junction that is formed between different parts within the same cell is called autotypic cell junction. Autotypic junction proteins form tight junctions found between membrane lamellae of a cell, especially in myelinating glial cells. Some of them have postsynaptic density-95/disks large/ zonula occludens-1 (PDZ) domains, which interact with the carboxyl (C)-terminal PDZ-binding motif of other proteins. PDZ domains are protein-protein interaction modules that play a role in protein complex assembly. The PDZ domain, which is widespread in bacteria, plants, yeast, metazoans, and Drosophila, allows the assembly of large multi-protein complexes. The multi-protein complexes act in intracellular signal transduction, protein targeting, and membrane polarization. The identified PDZ domain-containing proteins located at autotypic junctions include zonula occludens-1 (ZO-1), ZO-2, pals-1-associated tight junction protein (PATJ), multi-PDZ domain proteins (MUPPs), membrane-associated guanylate kinase inverted 2 (MAGI2), and protease-activated receptor (PAR)-3. PAR-3 interacts with atypical protein kinase C and PAR-6, forming a ternary complex, which plays an important role in the regulation of cell polarity. MAGI2 interacts with α-amino-3-hydroxyl-5-methyl-4-isoxazole propionate (AMPA) receptor at excitatory synapses. PATJ is detected in paranodal loops associated with claudin-1. On the other hand, MUPP1 is found in mesaxons and Schmidt-Lanterman incisures with claudin-5. ZO-1, ZO-2, and PAR-3 are found at all three sites. Different distributions of PDZ domain-containing proteins affect the development of autotypic junctions. In this review, we will describe PDZ domain-containing proteins at autotypic tight junctions in myelinating Schwann cells and their roles.

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ZO-1 Knockout by TALEN-Mediated Gene Targeting in MDCK Cells: Involvement of ZO-1 in the Regulation of Cytoskeleton and Cell Shape

Cited by 82 publications

References 40 publications

Effects of Osmolality on Paracellular Transport in MDCK II Cells

Effects of Osmolality on Paracellular Transport in MDCK II Cells

ZO‐2, a tight junction protein involved in gene expression, proliferation, apoptosis, and cell size regulation

PDZ Domain-containing Proteins at Autotypic Junctions in Myelinating Schwann Cells

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