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Article ; Online: A short guide to the tight junction.

Citi, Sandra / Fromm, Michael / Furuse, Mikio / González-Mariscal, Lorenza / Nusrat, Asma / Tsukita, Sachiko / Turner, Jerrold R

Journal of cell science

2024 Volume 137, Issue 9

Abstract: Tight junctions (TJs) are specialized regions of contact between cells of epithelial and endothelial tissues that form selective semipermeable paracellular barriers that establish and maintain body compartments with different fluid compositions. As such, ...

Abstract	Tight junctions (TJs) are specialized regions of contact between cells of epithelial and endothelial tissues that form selective semipermeable paracellular barriers that establish and maintain body compartments with different fluid compositions. As such, the formation of TJs represents a critical step in metazoan evolution, allowing the formation of multicompartmental organisms and true, barrier-forming epithelia and endothelia. In the six decades that have passed since the first observations of TJs by transmission electron microscopy, much progress has been made in understanding the structure, function, molecular composition and regulation of TJs. The goal of this Perspective is to highlight the key concepts that have emerged through this research and the future challenges that lie ahead for the field.
MeSH term(s)	Tight Junctions/metabolism ; Tight Junctions/ultrastructure ; Humans ; Animals ; Epithelial Cells/metabolism ; Epithelial Cells/ultrastructure ; Epithelial Cells/cytology
Language	English
Publishing date	2024-05-07
Publishing country	England
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.261776
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Zs.MG 14: Show issues

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Article ; Online: Parallel cryo electron tomography on in situ lamellae.

Eisenstein, Fabian / Yanagisawa, Haruaki / Kashihara, Hiroka / Kikkawa, Masahide / Tsukita, Sachiko / Danev, Radostin

Nature methods

2022 Volume 20, Issue 1, Page(s) 131–138

Abstract: In situ cryo electron tomography of cryo focused ion beam milled samples has emerged in recent years as a powerful technique for structural studies of macromolecular complexes in their native cellular environment. However, the possibilities for recording ...

Abstract	In situ cryo electron tomography of cryo focused ion beam milled samples has emerged in recent years as a powerful technique for structural studies of macromolecular complexes in their native cellular environment. However, the possibilities for recording tomographic tilt series in a high-throughput manner are limited, in part by the lamella-shaped samples. Here we utilize a geometrical sample model and optical image shift to record tens of tilt series in parallel, thereby saving time and gaining access to sample areas conventionally used for tracking specimen movement. The parallel cryo electron tomography (PACE-tomo) method achieves a throughput faster than 5 min per tilt series and allows for the collection of sample areas that were previously unreachable, thus maximizing the amount of data from each lamella. Performance testing with ribosomes in vitro and in situ on state-of-the-art and general-purpose microscopes demonstrated the high throughput and quality of PACE-tomo.
MeSH term(s)	Electron Microscope Tomography/methods ; Cryoelectron Microscopy/methods ; Macromolecular Substances/chemistry ; Ribosomes
Chemical Substances	Macromolecular Substances
Language	English
Publishing date	2022-12-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2169522-2
ISSN	1548-7105 ; 1548-7091
ISSN (online)	1548-7105
ISSN	1548-7091
DOI	10.1038/s41592-022-01690-1
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Article ; Online: Reciprocal Association between the Apical Junctional Complex and AMPK: A Promising Therapeutic Target for Epithelial/Endothelial Barrier Function?

Tsukita, Kazuto / Yano, Tomoki / Tamura, Atsushi / Tsukita, Sachiko

International journal of molecular sciences

2019 Volume 20, Issue 23

Abstract: Epithelial/endothelial cells adhere to each other via cell-cell junctions including tight junctions (TJs) and adherens junctions (AJs). TJs and AJs are spatiotemporally and functionally integrated, and are thus often collectively defined as apical ... ...

Abstract	Epithelial/endothelial cells adhere to each other via cell-cell junctions including tight junctions (TJs) and adherens junctions (AJs). TJs and AJs are spatiotemporally and functionally integrated, and are thus often collectively defined as apical junctional complexes (AJCs), regulating a number of spatiotemporal events including paracellular barrier, selective permeability, apicobasal cell polarity, mechano-sensing, intracellular signaling cascades, and epithelial morphogenesis. Over the past 15 years, it has been acknowledged that adenosine monophosphate (AMP)-activated protein kinase (AMPK), a well-known central regulator of energy metabolism, has a reciprocal association with AJCs. Here, we review the current knowledge of this association and show the following evidences: (1) as an upstream regulator, AJs activate the liver kinase B1 (LKB1)-AMPK axis particularly in response to applied junctional tension, and (2) TJ function and apicobasal cell polarization are downstream targets of AMPK and are promoted by AMPK activation. Although molecular mechanisms underlying these phenomena have not yet been completely elucidated, identifications of novel AMPK effectors in AJCs and AMPK-driven epithelial transcription factors have enhanced our knowledge. More intensive studies along this line would eventually lead to the development of AMPK-based therapies, enabling us to manipulate epithelial/endothelial barrier function.
MeSH term(s)	AMP-Activated Protein Kinases/metabolism ; Adherens Junctions/metabolism ; Animals ; Cell Polarity ; Endothelial Cells/cytology ; Endothelial Cells/metabolism ; Energy Metabolism ; Epithelial Cells/cytology ; Epithelial Cells/metabolism ; Humans ; Permeability ; Signal Transduction ; Tight Junctions/metabolism
Chemical Substances	AMP-Activated Protein Kinases (EC 2.7.11.31)
Language	English
Publishing date	2019-11-29
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms20236012
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Article ; Online: Claudin-2 upregulation enhances intestinal permeability, immune activation, dysbiosis, and mortality in sepsis.

Oami, Takehiko / Abtahi, Shabnam / Shimazui, Takashi / Chen, Ching-Wen / Sweat, Yan Y / Liang, Zhe / Burd, Eileen M / Farris, Alton B / Roland, Joe T / Tsukita, Sachiko / Ford, Mandy L / Turner, Jerrold R / Coopersmith, Craig M

Proceedings of the National Academy of Sciences of the United States of America

2024 Volume 121, Issue 10, Page(s) e2217877121

Abstract: Intestinal epithelial expression of the tight junction protein claudin-2, which forms paracellular cation and water channels, is precisely regulated during development and in disease. Here, we show that small intestinal epithelial claudin-2 expression is ...

Abstract	Intestinal epithelial expression of the tight junction protein claudin-2, which forms paracellular cation and water channels, is precisely regulated during development and in disease. Here, we show that small intestinal epithelial claudin-2 expression is selectively upregulated in septic patients. Similar changes occurred in septic mice, where claudin-2 upregulation coincided with increased flux across the paracellular pore pathway. In order to define the significance of these changes, sepsis was induced in claudin-2 knockout (KO) and wild-type (WT) mice. Sepsis-induced increases in pore pathway permeability were prevented by claudin-2 KO. Moreover, claudin-2 deletion reduced interleukin-17 production and T cell activation and limited intestinal damage. These effects were associated with reduced numbers of neutrophils, macrophages, dendritic cells, and bacteria within the peritoneal fluid of septic claudin-2 KO mice. Most strikingly, claudin-2 deletion dramatically enhanced survival in sepsis. Finally, the microbial changes induced by sepsis were less pathogenic in claudin-2 KO mice as survival of healthy WT mice injected with cecal slurry collected from WT mice 24 h after sepsis was far worse than that of healthy WT mice injected with cecal slurry collected from claudin-2 KO mice 24 h after sepsis. Claudin-2 upregulation and increased pore pathway permeability are, therefore, key intermediates that contribute to development of dysbiosis, intestinal damage, inflammation, ineffective pathogen control, and increased mortality in sepsis. The striking impact of claudin-2 deletion on progression of the lethal cascade activated during sepsis suggests that claudin-2 may be an attractive therapeutic target in septic patients.
MeSH term(s)	Animals ; Humans ; Mice ; Claudin-2/genetics ; Claudin-2/metabolism ; Dysbiosis/genetics ; Dysbiosis/metabolism ; Intestinal Barrier Function ; Intestinal Mucosa/metabolism ; Permeability ; Sepsis/metabolism ; Tight Junctions/metabolism ; Up-Regulation
Chemical Substances	Claudin-2 ; Cldn2 protein, mouse
Language	English
Publishing date	2024-02-27
Publishing country	United States
Document type	Journal Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2217877121
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Zs.A 1148: Show issues

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Article ; Online: Publisher Correction: AMPK-dependent phosphorylation of cingulin reversibly regulates its binding to actin filaments and microtubules.

Yano, Tomoki / Torisawa, Takayuki / Oiwa, Kazuhiro / Tsukita, Sachiko

Scientific reports

2018 Volume 8, Issue 1, Page(s) 17991

Abstract: A correction to this article has been published and is linked from the HTML and PDF versions of this paper. The error has been fixed in the paper. ...

Abstract	A correction to this article has been published and is linked from the HTML and PDF versions of this paper. The error has been fixed in the paper.
Language	English
Publishing date	2018-12-17
Publishing country	England
Document type	Published Erratum
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-018-37079-4
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Article ; Online: AMPK-dependent phosphorylation of cingulin reversibly regulates its binding to actin filaments and microtubules.

Yano, Tomoki / Torisawa, Takayuki / Oiwa, Kazuhiro / Tsukita, Sachiko

Scientific reports

2018 Volume 8, Issue 1, Page(s) 15550

Abstract: Cytoskeletal organization is essential for the precise morphogenesis of cells, tissues, and organs. Cytoskeletons, bound to scaffolding proteins, regulate the apical junction complex (AJC), which is composed of tight and adherens junctions, and located ... ...

Abstract	Cytoskeletal organization is essential for the precise morphogenesis of cells, tissues, and organs. Cytoskeletons, bound to scaffolding proteins, regulate the apical junction complex (AJC), which is composed of tight and adherens junctions, and located at the apical side of epithelial cell sheets. Cingulin is a tight junction-associated protein that binds to both actin filaments and microtubules. However, how cingulin binds to microtubules and whether cingulin can bind to actin and microtubules simultaneously are unclear. Here we examined the mechanisms behind cingulin's cytoskeleton-binding properties. First, using total internal reflection fluorescence microscopy, we detected cingulin at microtubule cross points. We then found the interdomain interactions in cingulin molecules. Notably, we found that this interaction was regulated by AMPK-dependent phosphorylation and changed cingulin's conformation and binding properties to actin filaments and microtubules. Finally, we found that the AMPK-regulated cingulin properties regulated the barrier functions of epithelial cell sheets. We propose that the cellular metabolic state, which involves AMPK, can contribute to the organization and maintenance of epithelial tissues through cingulin's tight junction/cytoskeleton regulation.
MeSH term(s)	AMP-Activated Protein Kinases/metabolism ; Actin Cytoskeleton/metabolism ; Animals ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Mice ; Microscopy, Fluorescence ; Microtubules/metabolism ; Phosphorylation ; Protein Binding ; Protein Conformation ; Protein Processing, Post-Translational
Chemical Substances	Cgn protein, mouse ; Membrane Proteins ; AMP-Activated Protein Kinases (EC 2.7.11.31)
Language	English
Publishing date	2018-10-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-018-33418-7
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Article: The Claudins: From Tight Junctions to Biological Systems.

Tsukita, Sachiko / Tanaka, Hiroo / Tamura, Atsushi

Trends in biochemical sciences

2018 Volume 44, Issue 2, Page(s) 141–152

Abstract: Claudins are cell-cell adhesion molecules located at the tight junctions (TJs) between cells in epithelial cell sheets. The claudin family in mammals consists of 27 four-transmembrane domain proteins. Claudins are responsible for the paracellular barrier ...

Abstract	Claudins are cell-cell adhesion molecules located at the tight junctions (TJs) between cells in epithelial cell sheets. The claudin family in mammals consists of 27 four-transmembrane domain proteins. Claudins are responsible for the paracellular barrier function of TJs, and in some cases confer paracellular channel functions to the paracellular barriers of TJs. Based on recent breakthroughs in the molecular structure of claudins, the hypothetical 'antiparallel double row model' was proposed, which suggests how claudins polymerize in a linear fashion and form TJ strands with paracellular barrier and channel functions. Meanwhile, ongoing studies at the cell and tissue levels are clarifying how the paracellular barrier and/or channel functions of claudin-based TJs, which are both robust and flexible, organize various biological systems.
MeSH term(s)	Animals ; Claudins/metabolism ; Epithelial Cells/metabolism ; Humans ; Tight Junctions/metabolism
Chemical Substances	Claudins
Language	English
Publishing date	2018-10-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	194216-5
ISSN	1362-4326 ; 0968-0004 ; 0376-5067
ISSN (online)	1362-4326
ISSN	0968-0004 ; 0376-5067
DOI	10.1016/j.tibs.2018.09.008
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Zs.A 1207: Show issues

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Article ; Online: R40.76 binds to the α domain of ZO-1: role of ZO-1 (α+) in epithelial differentiation and mechano-sensing.

Rouaud, Florian / Vasileva, Ekaterina / Spadaro, Domenica / Tsukita, Sachiko / Citi, Sandra

Tissue barriers

2019 Volume 7, Issue 3, Page(s) e1653748

Abstract: The barrier function of epithelia and endothelia depends on tight junctions, which are formed by the polymerization of claudins on a scaffold of ZO proteins. Two differentially spliced isoforms of ZO-1 have been described, depending on the presence of ... ...

Abstract	The barrier function of epithelia and endothelia depends on tight junctions, which are formed by the polymerization of claudins on a scaffold of ZO proteins. Two differentially spliced isoforms of ZO-1 have been described, depending on the presence of the α domain, but the function of this domain is unclear. ZO-1 also contains a C-terminal ZU5 domain, which is involved in a mechano-sensitive intramolecular interaction with the central (ZPSG) region of ZO-1. Here we use immunoblotting and immunofluorescence to map the binding sites for commercially available monoclonal and polyclonal antibodies against ZO-1, and for a new polyclonal antibody (R3) that we developed against the ZO-1 C-terminus. We demonstrate that antibody R40.76 binds to the α domain, and the R3 antibody binds to the ZU5 domain. The (α+) isoform of ZO-1 shows higher expression in epithelial versus endothelial cells, and in differentiated versus undifferentiated primary keratinocytes, suggesting a link to epithelial differentiation and a potential molecular adaptation to junctions subjected to stronger mechanical forces. These results provide new tools and hypotheses to investigate the role of the α and ZU5 domains in ZO-1 mechano-sensing and dynamic interactions with the cytoskeleton and junctional ligands.
MeSH term(s)	Animals ; Cell Differentiation ; Epithelium/metabolism ; Humans ; Keratinocytes/metabolism ; Tight Junctions/metabolism ; Zonula Occludens-1 Protein/physiology
Chemical Substances	Zonula Occludens-1 Protein
Language	English
Publishing date	2019-08-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2168-8370
ISSN (online)	2168-8370
DOI	10.1080/21688370.2019.1653748
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Article ; Online: Dual-color live imaging unveils stepwise organization of multiple basal body arrays by cytoskeletons.

Shiratsuchi, Gen / Konishi, Satoshi / Yano, Tomoki / Yanagihashi, Yuichi / Nakayama, Shogo / Katsuno, Tatsuya / Kashihara, Hiroka / Tanaka, Hiroo / Tsukita, Kazuto / Suzuki, Koya / Herawati, Elisa / Watanabe, Hitomi / Hirai, Toyohiro / Yagi, Takeshi / Kondoh, Gen / Gotoh, Shimpei / Tamura, Atsushi / Tsukita, Sachiko

EMBO reports

2024 Volume 25, Issue 3, Page(s) 1176–1207

Abstract: For mucociliary clearance of pathogens, tracheal multiciliated epithelial cells (MCCs) organize coordinated beating of cilia, which originate from basal bodies (BBs) with basal feet (BFs) on one side. To clarify the self-organizing mechanism of ... ...

Abstract	For mucociliary clearance of pathogens, tracheal multiciliated epithelial cells (MCCs) organize coordinated beating of cilia, which originate from basal bodies (BBs) with basal feet (BFs) on one side. To clarify the self-organizing mechanism of coordinated intracellular BB-arrays composed of a well-ordered BB-alignment and unidirectional BB-orientation, determined by the direction of BB to BF, we generated double transgenic mice with GFP-centrin2-labeled BBs and mRuby3-Cep128-labeled BFs for long-term, high-resolution, dual-color live-cell imaging in primary-cultured tracheal MCCs. At early timepoints of MCC differentiation, BB-orientation and BB-local alignment antecedently coordinated in an apical microtubule-dependent manner. Later during MCC differentiation, fluctuations in BB-orientation were restricted, and locally aligned BB-arrays were further coordinated to align across the entire cell (BB-global alignment), mainly in an apical intermediate-sized filament-lattice-dependent manner. Thus, the high coordination of the BB-array was established for efficient mucociliary clearance as the primary defense against pathogen infection, identifying apical cytoskeletons as potential therapeutic targets.
MeSH term(s)	Mice ; Animals ; Basal Bodies ; Cytoskeleton ; Microtubules ; Cilia ; Epithelial Cells
Language	English
Publishing date	2024-02-05
Publishing country	England
Document type	Journal Article
ZDB-ID	2020896-0
ISSN	1469-3178 ; 1469-221X
ISSN (online)	1469-3178
ISSN	1469-221X
DOI	10.1038/s44319-024-00066-0
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Zs.A 5433: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Paracellular barrier and channel functions of TJ claudins in organizing biological systems: advances in the field of barriology revealed in knockout mice.

Tamura, Atsushi / Tsukita, Sachiko

Seminars in cell & developmental biology

2014 Volume 36, Page(s) 177–185

Abstract: Claudin was first identified as a four-transmembrane protein in the tight junctions (TJs) between epithelial cells. The claudin family has 27 members, which are specifically expressed depending on the epithelial cell type. Accumulating evidence has ... ...

Abstract	Claudin was first identified as a four-transmembrane protein in the tight junctions (TJs) between epithelial cells. The claudin family has 27 members, which are specifically expressed depending on the epithelial cell type. Accumulating evidence has revealed that claudins are responsible for the paracellular barrier that prevents molecules from passing through epithelial cell sheets. In addition, the extracellular domains of some claudins enable them to act as a permselective paracellular channel for specific molecules, including ions and/or non-ionic solutes. Recent studies using claudin knockout mice revealed that the loss of claudins' specific paracellular barrier and/or channel functions affects specific biological functions and leads to pathological states. In this review, considering recent findings in vivo, we describe how, sometimes in concert with canonical transporters and channels, the paracellular barrier and channel functions of claudins sophisticatedly organize biological systems.
MeSH term(s)	Animals ; Biological Transport ; Blood-Brain Barrier/physiology ; Central Nervous System/physiology ; Claudins/genetics ; Claudins/metabolism ; Ear, Inner/physiology ; Epithelium/physiology ; Gastrointestinal Tract/physiology ; Ion Channels ; Kidney/physiology ; Mice ; Mice, Knockout ; Tight Junctions/physiology ; Water
Chemical Substances	Claudins ; Ion Channels ; Water (059QF0KO0R)
Language	English
Publishing date	2014-12
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1312473-0
ISSN	1096-3634 ; 1084-9521
ISSN (online)	1096-3634
ISSN	1084-9521
DOI	10.1016/j.semcdb.2014.09.019
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