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Article ; Online: The novel membrane protein Hoka regulates septate junction organization and stem cell homeostasis in the

Izumi, Yasushi / Furuse, Kyoko / Furuse, Mikio

2021 Volume 134, Issue 6

Abstract: Smooth septate junctions (sSJs) regulate the paracellular transport in the intestinal tract in arthropods. ... ...

Abstract	Smooth septate junctions (sSJs) regulate the paracellular transport in the intestinal tract in arthropods. In
Language	English
Publishing date	2021-03-26
Publishing country	England
Document type	Journal Article ; 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.257022
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Article ; Online: Recent advances in understanding tight junctions.

Furuse, Mikio / Takai, Yoshimi

Faculty reviews

2021 Volume 10, Page(s) 18

Abstract: Tight junctions (TJs) are one type of cell-cell junction in epithelial cell types in vertebrates. They form a paracellular diffusion barrier and create the boundary between the apical and basolateral plasma membrane domains. The molecular constituents of ...

Abstract	Tight junctions (TJs) are one type of cell-cell junction in epithelial cell types in vertebrates. They form a paracellular diffusion barrier and create the boundary between the apical and basolateral plasma membrane domains. The molecular constituents of TJs have mostly been identified, and now their cell biology has shifted to understanding of their formation, dynamics, and functional regulation as well as their relationship to the organization of epithelial cells. Accumulating novel findings are supported by new methods, including super-resolution microscopy, quantitative microscopy, biophysical measurements, and genome editing-mediated gene manipulation. As a conceptual breakthrough, liquid-liquid phase separation seems to be involved in the formation of TJs as super-molecular complexes. This short article summarizes seminal studies in the cell biology of TJs from the last three years.
Language	English
Publishing date	2021-02-23
Publishing country	England
Document type	Journal Article ; Review
ISSN	2732-432X
ISSN (online)	2732-432X
DOI	10.12703/r/10-18
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Article ; Online: Integrating Continuous Transepithelial Flux Measurements into an Ussing Chamber Set-Up.

Alija, Çlirim / Knobe, Lukas / Pouyiourou, Ioanna / Furuse, Mikio / Rosenthal, Rita / Günzel, Dorothee

International journal of molecular sciences

2024 Volume 25, Issue 4

Abstract: Fluorescently labelled compounds are often employed to study the paracellular properties of epithelia. For flux measurements, these compounds are added to the donor compartment and samples collected from the acceptor compartment at regular intervals. ... ...

Abstract	Fluorescently labelled compounds are often employed to study the paracellular properties of epithelia. For flux measurements, these compounds are added to the donor compartment and samples collected from the acceptor compartment at regular intervals. However, this method fails to detect rapid changes in permeability. For continuous transepithelial flux measurements in an Ussing chamber setting, a device was developed, consisting of a flow-through chamber with an attached LED, optical filter, and photodiode, all encased in a light-impermeable container. The photodiode output was amplified and recorded. Calibration with defined fluorescein concentration (range of 1 nM to 150 nM) resulted in a linear output. As proof of principle, flux measurements were performed on various cell lines. The results confirmed a linear dependence of the flux on the fluorescein concentration in the donor compartment. Flux depended on paracellular barrier function (expression of specific tight junction proteins, and EGTA application to induce barrier loss), whereas activation of transcellular chloride secretion had no effect on fluorescein flux. Manipulation of the lateral space by osmotic changes in the perfusion solution also affected transepithelial fluorescein flux. In summary, this device allows a continuous recording of transepithelial flux of fluorescent compounds in parallel with the electrical parameters recorded by the Ussing chamber.
MeSH term(s)	Tight Junctions/metabolism ; Epithelium ; Cell Line ; Tight Junction Proteins/metabolism ; Fluorescein/metabolism
Chemical Substances	Tight Junction Proteins ; Fluorescein (TPY09G7XIR)
Language	English
Publishing date	2024-02-13
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms25042252
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Article ; Online: Bicellular Localization of Tricellular Junctional Protein Angulin-3/ILDR2 Allows Detection of Podocyte Injury.

Higashi, Atsuko Y / Saito, Akira C / Higashi, Tomohito / Furuse, Kyoko / Furuse, Mikio / Chiba, Hideki / Kazama, Junichiro J

The American journal of pathology

2024 Volume 194, Issue 5, Page(s) 673–683

Abstract: Podocytes serve as part of the renal filtration unit with slit diaphragms. Although the structure of slit diaphragms between two cells is well characterized, how the tricellular contact of podocytes is organized and how it changes in injured podocytes ... ...

Abstract	Podocytes serve as part of the renal filtration unit with slit diaphragms. Although the structure of slit diaphragms between two cells is well characterized, how the tricellular contact of podocytes is organized and how it changes in injured podocytes remains unknown. This study focused on a tricellular junction protein, angulin-3, and its localization in healthy podocytes, in developmental stages, and in pathologic conditions, using a newly established monoclonal antibody. Angulin-3 was confined at tricellular junctions of primordial podocytes, then transiently localized at bicellular junctions as foot process interdigitation developed and the intercellular junctions rearranged into slit diaphragm, and eventually distributed in a sparse punctate pattern on the foot processes of adult podocytes. In the rodent podocyte injury models, angulin-3 showed bicellular localization between the foot processes, and the localization turned from punctate to dashed linear pattern along the effaced foot processes with the progression of podocyte injury. Angulin-3 also accumulated between foot processes in a linear pattern in kidney biopsy samples of human nephrotic syndrome. Additionally, the line length of angulin-3 staining signal correlated with risk of relapse under glucocorticoid therapy in patients with minimal change nephrotic syndrome. This study proposes an image program to score the linearity of the accumulation pattern of angulin-3 to evaluate the relapse risk of patients with minimal change nephrotic syndrome.
MeSH term(s)	Adult ; Humans ; Podocytes/metabolism ; Tight Junctions/pathology ; Nephrosis, Lipoid/metabolism ; Nephrosis, Lipoid/pathology ; Intercellular Junctions/metabolism ; Recurrence
Language	English
Publishing date	2024-02-02
Publishing country	United States
Document type	Journal Article
ZDB-ID	2943-9
ISSN	1525-2191 ; 0002-9440
ISSN (online)	1525-2191
ISSN	0002-9440
DOI	10.1016/j.ajpath.2024.01.008
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Article ; Online: Tight Junction Structure and Function Revisited: (Trends in Cell Biology 30, 805-817, 2020).

Otani, Tetsuhisa / Furuse, Mikio

Trends in cell biology

2020 Volume 30, Issue 12, Page(s) 1014

Language	English
Publishing date	2020-10-20
Publishing country	England
Document type	Published Erratum
ZDB-ID	30122-x
ISSN	1879-3088 ; 0962-8924
ISSN (online)	1879-3088
ISSN	0962-8924
DOI	10.1016/j.tcb.2020.10.001
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Article ; Online: Tight Junction Structure and Function Revisited.

Otani, Tetsuhisa / Furuse, Mikio

Trends in cell biology

2020 Volume 30, Issue 10, Page(s) 805–817

Abstract: Tight junctions (TJs) are intercellular junctions critical for building the epithelial barrier and maintaining epithelial polarity. The claudin family of membrane proteins play central roles in TJ structure and function. However, recent findings have ... ...

Abstract	Tight junctions (TJs) are intercellular junctions critical for building the epithelial barrier and maintaining epithelial polarity. The claudin family of membrane proteins play central roles in TJ structure and function. However, recent findings have uncovered claudin-independent aspects of TJ structure and function, and additional players including junctional adhesion molecules (JAMs), membrane lipids, phase separation of the zonula occludens (ZO) family of scaffolding proteins, and mechanical force have been shown to play important roles in TJ structure and function. In this review, we discuss how these new findings have the potential to transform our understanding of TJ structure and function, and how the intricate network of TJ proteins and membrane lipids dynamically interact to drive TJ assembly.
MeSH term(s)	Animals ; Cell Polarity ; Epithelial Cells/cytology ; Epithelial Cells/metabolism ; Humans ; Models, Biological ; Tight Junctions/chemistry ; Tight Junctions/metabolism
Language	English
Publishing date	2020-09-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	30122-x
ISSN	1879-3088 ; 0962-8924
ISSN (online)	1879-3088
ISSN	0962-8924
DOI	10.1016/j.tcb.2020.08.004
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Article ; Online: Mechanism of interdigitation formation at apical boundary of MDCK cell.

Miyazaki, Shintaro / Otani, Tetsuhisa / Sugihara, Kei / Fujimori, Toshihiko / Furuse, Mikio / Miura, Takashi

iScience

2023 Volume 26, Issue 5, Page(s) 106594

Abstract: It has been reported that the MDCK cell tight junction shows stochastic fluctuation and forms the interdigitation structure, but the mechanism of the pattern formation remains to be elucidated. In the present study, we first quantified the shape of the ... ...

Abstract	It has been reported that the MDCK cell tight junction shows stochastic fluctuation and forms the interdigitation structure, but the mechanism of the pattern formation remains to be elucidated. In the present study, we first quantified the shape of the cell-cell boundary at the initial phase of pattern formation. We found that the Fourier transform of the boundary shape shows linearity in the log-log plot, indicating the existence of scaling. Next, we tested several working hypotheses and found that the Edwards-Wilkinson equation, which consists of stochastic movement and boundary shortening, can reproduce the scaling property. Next, we examined the molecular nature of stochastic movement and found that myosin light chain puncta may be responsible. Quantification of boundary shortening indicates that mechanical property change may also play some role. Physiological meaning and scaling properties of the cell-cell boundary are discussed.
Language	English
Publishing date	2023-04-21
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2023.106594
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Article ; Online: Tight junction membrane proteins regulate the mechanical resistance of the apical junctional complex.

Nguyen, Thanh Phuong / Otani, Tetsuhisa / Tsutsumi, Motosuke / Kinoshita, Noriyuki / Fujiwara, Sachiko / Nemoto, Tomomi / Fujimori, Toshihiko / Furuse, Mikio

The Journal of cell biology

2024 Volume 223, Issue 5

Abstract: Epithelia must be able to resist mechanical force to preserve tissue integrity. While intercellular junctions are known to be important for the mechanical resistance of epithelia, the roles of tight junctions (TJs) remain to be established. We previously ...

Abstract	Epithelia must be able to resist mechanical force to preserve tissue integrity. While intercellular junctions are known to be important for the mechanical resistance of epithelia, the roles of tight junctions (TJs) remain to be established. We previously demonstrated that epithelial cells devoid of the TJ membrane proteins claudins and JAM-A completely lack TJs and exhibit focal breakages of their apical junctions. Here, we demonstrate that apical junctions fracture when claudin/JAM-A-deficient cells undergo spontaneous cell stretching. The junction fracture was accompanied by actin disorganization, and actin polymerization was required for apical junction integrity in the claudin/JAM-A-deficient cells. Further deletion of CAR resulted in the disruption of ZO-1 molecule ordering at cell junctions, accompanied by severe defects in apical junction integrity. These results demonstrate that TJ membrane proteins regulate the mechanical resistance of the apical junctional complex in epithelial cells.
MeSH term(s)	Actins/genetics ; Actins/metabolism ; Claudins/metabolism ; Epithelial Cells/metabolism ; Intercellular Junctions/genetics ; Intercellular Junctions/metabolism ; Tight Junction Proteins/metabolism ; Tight Junctions/metabolism ; Madin Darby Canine Kidney Cells ; Animals ; Dogs
Chemical Substances	Actins ; Claudins ; Tight Junction Proteins
Language	English
Publishing date	2024-03-22
Publishing country	United States
Document type	Journal Article
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202307104
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Article ; Online: Angulin-1 seals tricellular contacts independently of tricellulin and claudins.

Sugawara, Taichi / Furuse, Kyoko / Otani, Tetsuhisa / Wakayama, Tomohiko / Furuse, Mikio

The Journal of cell biology

2021 Volume 220, Issue 9

Abstract: Tricellular tight junctions (tTJs) are specialized tight junctions (TJs) that seal the intercellular space at tricellular contacts (TCs), where the vertices of three epithelial cells meet. Tricellulin and angulin family membrane proteins are known ... ...

Abstract	Tricellular tight junctions (tTJs) are specialized tight junctions (TJs) that seal the intercellular space at tricellular contacts (TCs), where the vertices of three epithelial cells meet. Tricellulin and angulin family membrane proteins are known constituents of tTJs, but the molecular mechanism of tTJ formation remains elusive. Here, we investigated the roles of angulin-1 and tricellulin in tTJ formation in MDCK II cells by genome editing. Angulin-1-deficient cells lost the plasma membrane contact at TCs with impaired epithelial barrier function. The C terminus of angulin-1 bound to the TJ scaffold protein ZO-1, and disruption of their interaction influenced the localization of claudins at TCs, but not the tricellular sealing. Strikingly, the plasma membrane contact at TCs was formed in tricellulin- or claudin-deficient cells. These findings demonstrate that angulin-1 is responsible for the plasma membrane seal at TCs independently of tricellulin and claudins.
MeSH term(s)	Animals ; Binding Sites ; Claudin-2/genetics ; Claudin-2/metabolism ; Dogs ; Extracellular Space/metabolism ; Gene Editing ; Gene Expression Regulation ; Gene Knockout Techniques ; MARVEL Domain Containing 2 Protein/deficiency ; MARVEL Domain Containing 2 Protein/genetics ; Madin Darby Canine Kidney Cells ; Occludin/genetics ; Occludin/metabolism ; Protein Binding ; Protein Interaction Domains and Motifs ; Receptors, Lipoprotein/deficiency ; Receptors, Lipoprotein/genetics ; Signal Transduction ; Tight Junctions/metabolism ; Tight Junctions/ultrastructure ; Transcription Factors/deficiency ; Transcription Factors/genetics ; Zonula Occludens-1 Protein/genetics ; Zonula Occludens-1 Protein/metabolism ; alpha Catenin/genetics ; alpha Catenin/metabolism
Chemical Substances	Claudin-2 ; MARVEL Domain Containing 2 Protein ; Occludin ; Receptors, Lipoprotein ; Transcription Factors ; Zonula Occludens-1 Protein ; alpha Catenin
Language	English
Publishing date	2021-07-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202005062
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Article ; Online: [Molecular organization of tricellular tight junctions].

Furuse, Mikio

Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan

2014 Volume 134, Issue 5, Page(s) 615–621

Abstract: Within an epithelial cellular sheet, the paracellular pathway can be divided into two routes: one between two adjacent cells and one at tricellular contacts, where the vertices of three cells meet. For epithelial barrier function, tight junctions ... ...

Abstract	Within an epithelial cellular sheet, the paracellular pathway can be divided into two routes: one between two adjacent cells and one at tricellular contacts, where the vertices of three cells meet. For epithelial barrier function, tight junctions restrict solute permeability through the paracellular pathway between two cells, while tricellular contacts contain specialized structures of tight junctions, named tricellular tight junctions (tTJs). Two types of membrane proteins, tricellulin and angulin family proteins (angulin-1/LSR, angulin-2/ILDR1 and angulin-3/ILDR2) have been identified as molecular components of tTJs. Angulins recruit triellulin to tTJs and these tTJ-associated proteins are required for normal tTJ formation as well as strong epithelial barrier function. Furthermore, mutations in tricellulin and angulin-2/ILDR1 genes cause autosomal recessive familial deafness, DFNB49 and DFNB42, respectively. Further analyses of the angulin-tricellulin system should lead to better understanding of the molecular mechanism and regulation of tTJs.
MeSH term(s)	Animals ; Cell Communication ; Epithelium/metabolism ; MARVEL Domain Containing 2 Protein/chemistry ; MARVEL Domain Containing 2 Protein/metabolism ; Signal Transduction ; Tight Junctions/metabolism
Chemical Substances	MARVEL Domain Containing 2 Protein
Language	Japanese
Publishing date	2014-04-25
Publishing country	Japan
Document type	English Abstract ; Journal Article ; Review
ZDB-ID	200514-1
ISSN	1347-5231 ; 0031-6903 ; 0372-7750 ; 0919-2085 ; 0919-2131
ISSN (online)	1347-5231
ISSN	0031-6903 ; 0372-7750 ; 0919-2085 ; 0919-2131
DOI	10.1248/yakushi.14-00006-1
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