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Article ; Online: The ACE2 Receptor for Coronavirus Entry Is Localized at Apical Cell-Cell Junctions of Epithelial Cells.

Rouaud, Florian / Méan, Isabelle / Citi, Sandra

2022 Volume 11, Issue 4

Abstract: Transmembrane proteins of adherens and tight junctions are known targets for viruses and bacterial toxins. The coronavirus receptor ACE2 has been localized at the apical surface of epithelial cells, but it is not clear whether ACE2 is localized at apical ...

Abstract	Transmembrane proteins of adherens and tight junctions are known targets for viruses and bacterial toxins. The coronavirus receptor ACE2 has been localized at the apical surface of epithelial cells, but it is not clear whether ACE2 is localized at apical Cell-Cell junctions and whether it associates with junctional proteins. Here we explored the expression and localization of ACE2 and its association with transmembrane and tight junction proteins in epithelial tissues and cultured cells by data mining, immunoblotting, immunofluorescence microscopy, and co-immunoprecipitation experiments. ACE2 mRNA is abundant in epithelial tissues, where its expression correlates with the expression of the tight junction proteins cingulin and occludin. In cultured epithelial cells ACE2 mRNA is upregulated upon differentiation and ACE2 protein is widely expressed and co-immunoprecipitates with the transmembrane proteins ADAM17 and CD9. We show by immunofluorescence microscopy that ACE2 colocalizes with ADAM17 and CD9 and the tight junction protein cingulin at apical junctions of intestinal (Caco-2), mammary (Eph4) and kidney (mCCD) epithelial cells. These observations identify ACE2, ADAM17 and CD9 as new epithelial junctional transmembrane proteins and suggest that the cytokine-enhanced endocytic internalization of junction-associated protein complexes comprising ACE2 may promote coronavirus entry.
MeSH term(s)	ADAM17 Protein/metabolism ; Adherens Junctions/metabolism ; Angiotensin-Converting Enzyme 2/genetics ; Angiotensin-Converting Enzyme 2/metabolism ; Cadherins/metabolism ; Carrier Proteins/metabolism ; Cell Line ; Cell Membrane Permeability ; Coronavirus/metabolism ; Epithelial Cells/metabolism ; Epithelial Cells/virology ; Gene Expression/genetics ; Intercellular Junctions/metabolism ; Intercellular Junctions/virology ; Tetraspanin 29/metabolism ; Tight Junction Proteins/metabolism ; Tight Junctions/metabolism ; Transcriptome/genetics
Chemical Substances	CD9 protein, human ; Cadherins ; Carrier Proteins ; Tetraspanin 29 ; Tight Junction Proteins ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23) ; ADAM17 Protein (EC 3.4.24.86) ; ADAM17 protein, human (EC 3.4.24.86)
Language	English
Publishing date	2022-02-11
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells11040627
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Article ; Online: The ACE2 Receptor for Coronavirus Entry Is Localized at Apical Cell—Cell Junctions of Epithelial Cells

Florian Rouaud / Isabelle Méan / Sandra Citi

Cells, Vol 11, Iss 627, p

2022 Volume 627

Abstract	Transmembrane proteins of adherens and tight junctions are known targets for viruses and bacterial toxins. The coronavirus receptor ACE2 has been localized at the apical surface of epithelial cells, but it is not clear whether ACE2 is localized at apical Cell—Cell junctions and whether it associates with junctional proteins. Here we explored the expression and localization of ACE2 and its association with transmembrane and tight junction proteins in epithelial tissues and cultured cells by data mining, immunoblotting, immunofluorescence microscopy, and co-immunoprecipitation experiments. ACE2 mRNA is abundant in epithelial tissues, where its expression correlates with the expression of the tight junction proteins cingulin and occludin. In cultured epithelial cells ACE2 mRNA is upregulated upon differentiation and ACE2 protein is widely expressed and co-immunoprecipitates with the transmembrane proteins ADAM17 and CD9. We show by immunofluorescence microscopy that ACE2 colocalizes with ADAM17 and CD9 and the tight junction protein cingulin at apical junctions of intestinal (Caco-2), mammary (Eph4) and kidney (mCCD) epithelial cells. These observations identify ACE2, ADAM17 and CD9 as new epithelial junctional transmembrane proteins and suggest that the cytokine-enhanced endocytic internalization of junction-associated protein complexes comprising ACE2 may promote coronavirus entry.
Keywords	ACE2 ; coronavirus ; Cell—Cell junctions ; epithelium ; Biology (General) ; QH301-705.5
Subject code	612
Language	English
Publishing date	2022-02-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article ; Online: The PLEKHA7-PDZD11 complex regulates the localization of the calcium pump PMCA and calcium handling in cultured cells.

Sluysmans, Sophie / Salmaso, Andrea / Rouaud, Florian / Méan, Isabelle / Brini, Marisa / Citi, Sandra

The Journal of biological chemistry

2022 Volume 298, Issue 8, Page(s) 102138

Abstract: The plasma membrane calcium ATPase (PMCA) extrudes calcium from the cytosol to the extracellular space to terminate calcium-dependent signaling. Although the distribution of PMCA is crucial for its function, the molecular mechanisms that regulate the ... ...

Abstract	The plasma membrane calcium ATPase (PMCA) extrudes calcium from the cytosol to the extracellular space to terminate calcium-dependent signaling. Although the distribution of PMCA is crucial for its function, the molecular mechanisms that regulate the localization of PMCA isoforms are not well understood. PLEKHA7 is implicated by genetic studies in hypertension and the regulation of calcium handling. PLEKHA7 recruits the small adapter protein PDZD11 to adherens junctions, and together they control the trafficking and localization of plasma membrane associated proteins, including the Menkes copper ATPase. Since PDZD11 binds to the C-terminal domain of b-isoforms of PMCA, PDZD11 and its interactor PLEKHA7 could control the localization and activity of PMCA. Here, we test this hypothesis using cultured cell model systems. We show using immunofluorescence microscopy and a surface biotinylation assay that KO of either PLEKHA7 or PDZD11 in mouse kidney collecting duct epithelial cells results in increased accumulation of endogenous PMCA at lateral cell-cell contacts and PDZ-dependent ectopic apical localization of exogenous PMCA4x/b isoform. In HeLa cells, coexpression of PDZD11 reduces membrane accumulation of overexpressed PMCA4x/b, and analysis of cytosolic calcium transients shows that PDZD11 counteracts calcium extrusion activity of overexpressed PMCA4x/b, but not PMCA4x/a, which lacks the PDZ-binding motif. Moreover, KO of PDZD11 in either endothelial (bEnd.3) or epithelial (mouse kidney collecting duct) cells increases the rate of calcium extrusion. Collectively, these results suggest that the PLEKHA7-PDZD11 complex modulates calcium homeostasis by regulating the localization of PMCA.
MeSH term(s)	Adherens Junctions/metabolism ; Animals ; Calcium/metabolism ; Carrier Proteins/metabolism ; Cells, Cultured ; HeLa Cells ; Humans ; Mice ; Plasma Membrane Calcium-Transporting ATPases/genetics ; Plasma Membrane Calcium-Transporting ATPases/metabolism ; Protein Isoforms/metabolism
Chemical Substances	Carrier Proteins ; PDZD11 protein, human ; PLEKHA7 protein, human ; Protein Isoforms ; Plasma Membrane Calcium-Transporting ATPases (EC 3.6.3.8) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2022-06-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2022.102138
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Article ; Online: Cooperative binding of the tandem WW domains of PLEKHA7 to PDZD11 promotes conformation-dependent interaction with tetraspanin 33.

Rouaud, Florian / Tessaro, Francesca / Aimaretti, Laura / Scapozza, Leonardo / Citi, Sandra

The Journal of biological chemistry

2020 Volume 295, Issue 28, Page(s) 9299–9312

Abstract: Pleckstrin homology domain-containing A7 (PLEKHA7) is a cytoplasmic protein at adherens junctions that has been implicated in hypertension, glaucoma, and responses ... ...

Abstract	Pleckstrin homology domain-containing A7 (PLEKHA7) is a cytoplasmic protein at adherens junctions that has been implicated in hypertension, glaucoma, and responses to
MeSH term(s)	Animals ; Carrier Proteins/chemistry ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cell Line ; Humans ; Hydrogen Bonding ; Mice ; Mice, Knockout ; Molecular Docking Simulation ; Protein Domains ; Protein Structure, Quaternary ; Tetraspanins/chemistry ; Tetraspanins/genetics ; Tetraspanins/metabolism
Chemical Substances	Carrier Proteins ; PDZD11 protein, human ; PLEKHA7 protein, human ; TSPAN33 protein, human ; Tetraspanins
Language	English
Publishing date	2020-05-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA120.012987
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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: Scaffolding proteins of vertebrate apical junctions: structure, functions and biophysics.

Rouaud, Florian / Sluysmans, Sophie / Flinois, Arielle / Shah, Jimit / Vasileva, Ekaterina / Citi, Sandra

Biochimica et biophysica acta. Biomembranes

2020 Volume 1862, Issue 10, Page(s) 183399

Abstract: Tight and adherens junctions are specialized sites of cell-cell interaction in epithelia and endothelia, and are involved in barrier, adhesion, and signaling functions. These functions are orchestrated by a highly organized meshwork of macromolecules in ... ...

Abstract	Tight and adherens junctions are specialized sites of cell-cell interaction in epithelia and endothelia, and are involved in barrier, adhesion, and signaling functions. These functions are orchestrated by a highly organized meshwork of macromolecules in the membrane and cytoplasmic compartments. In this review, we discuss the structural organization and functions of the major cytoplasmic scaffolding and adaptor proteins of vertebrate apical junctions (ZO proteins, afadin, PLEKHA7, cingulin, paracingulin, polarity complex proteins, and a few others), focusing on their interactions with cytoskeletal and signaling proteins. Furthermore, we discuss recent results highlighting how mechanical tension, protein-protein interactions and post-translational modifications regulate the conformation and function of scaffolding proteins, and how spontaneous phase separation into biomolecular condensates contributes to apical junction assembly. Using a sequence-based algorithm, a large fraction of cytoplasmic proteins of apical junctions are predicted to be phase separating proteins (PSPs), suggesting that formation of biomolecular condensates is a general mechanism to organize cell-cell contacts by clustering proteins.
MeSH term(s)	Animals ; Biophysical Phenomena ; Cytoplasm/metabolism ; Intercellular Junctions/metabolism ; Ligands ; Vertebrates/metabolism
Chemical Substances	Ligands
Language	English
Publishing date	2020-06-15
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	60-7
ISSN	1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamem.2020.183399
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Article ; Online: Cingulin and paracingulin tether myosins-2 to junctions to mechanoregulate the plasma membrane.

Rouaud, Florian / Huang, Wenmao / Flinois, Arielle / Jain, Kunalika / Vasileva, Ekaterina / Di Mattia, Thomas / Mauperin, Marine / Parry, David A D / Dugina, Vera / Chaponnier, Christine / Méan, Isabelle / Montessuit, Sylvie / Mutero-Maeda, Annick / Yan, Jie / Citi, Sandra

The Journal of cell biology

2023 Volume 222, Issue 7

Abstract: The mechanisms that regulate the spatial sorting of nonmuscle myosins-2 (NM2) isoforms and couple them mechanically to the plasma membrane are unclear. Here we show that the cytoplasmic junctional proteins cingulin (CGN) and paracingulin (CGNL1) interact ...

Abstract	The mechanisms that regulate the spatial sorting of nonmuscle myosins-2 (NM2) isoforms and couple them mechanically to the plasma membrane are unclear. Here we show that the cytoplasmic junctional proteins cingulin (CGN) and paracingulin (CGNL1) interact directly with NM2s through their C-terminal coiled-coil sequences. CGN binds strongly to NM2B, and CGNL1 to NM2A and NM2B. Knockout (KO), exogenous expression, and rescue experiments with WT and mutant proteins show that the NM2-binding region of CGN is required for the junctional accumulation of NM2B, ZO-1, ZO-3, and phalloidin-labeled actin filaments, and for the maintenance of tight junction membrane tortuosity and apical membrane stiffness. CGNL1 expression promotes the junctional accumulation of both NM2A and NM2B and its KO results in myosin-dependent fragmentation of adherens junction complexes. These results reveal a mechanism for the junctional localization of NM2A and NM2B and indicate that, by binding to NM2s, CGN and CGNL1 mechanically couple the actomyosin cytoskeleton to junctional protein complexes to mechanoregulate the plasma membrane.
MeSH term(s)	Adherens Junctions/metabolism ; Cell Membrane/metabolism ; Cytoskeletal Proteins/metabolism ; Cytoskeleton/metabolism ; Myosins/metabolism ; Tight Junctions/metabolism
Chemical Substances	Cytoskeletal Proteins ; Myosins (EC 3.6.4.1)
Language	English
Publishing date	2023-05-19
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.202208065
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Article ; Online: Cingulin binds to the ZU5 domain of scaffolding protein ZO-1 to promote its extended conformation, stabilization, and tight junction accumulation.

Vasileva, Ekaterina / Spadaro, Domenica / Rouaud, Florian / King, Jonathan M / Flinois, Arielle / Shah, Jimit / Sluysmans, Sophie / Méan, Isabelle / Jond, Lionel / Turner, Jerrold R / Citi, Sandra

The Journal of biological chemistry

2022 Volume 298, Issue 4, Page(s) 101797

Abstract: Zonula occludens-1 (ZO-1), the major scaffolding protein of tight junctions (TJs), recruits the cytoskeleton-associated proteins cingulin (CGN) and paracingulin (CGNL1) to TJs by binding to their N-terminal ZO-1 interaction motif. The conformation of ZO- ... ...

Abstract	Zonula occludens-1 (ZO-1), the major scaffolding protein of tight junctions (TJs), recruits the cytoskeleton-associated proteins cingulin (CGN) and paracingulin (CGNL1) to TJs by binding to their N-terminal ZO-1 interaction motif. The conformation of ZO-1 can be either folded or extended, depending on cytoskeletal tension and intramolecular and intermolecular interactions, and only ZO-1 in the extended conformation recruits the transcription factor DbpA to TJs. However, the sequences of ZO-1 that interact with CGN and CGNL1 and the role of TJ proteins in ZO-1 TJ assembly are not known. Here, we used glutathione-S-transferase pulldowns and immunofluorescence microscopy to show that CGN and CGNL1 bind to the C-terminal ZU5 domain of ZO-1 and that this domain is required for CGN and CGNL1 recruitment to TJs and to phase-separated ZO-1 condensates in cells. We show that KO of CGN, but not CGNL1, results in decreased accumulation of ZO-1 at TJs. Furthermore, ZO-1 lacking the ZU5 domain showed decreased accumulation at TJs, was detectable along lateral contacts, had a higher mobile fraction than full-length ZO-1 by fluorescence recovery after photobleaching analysis, and had a folded conformation, as determined by structured illumination microscopy of its N-terminal and C-terminal ends. The CGN-ZU5 interaction promotes the extended conformation of ZO-1, since binding of the CGN-ZO-1 interaction motif region to ZO-1 resulted in its interaction with DbpA in cells and in vitro. Together, these results show that binding of CGN to the ZU5 domain of ZO-1 promotes ZO-1 stabilization and accumulation at TJs by promoting its extended conformation.
MeSH term(s)	Cytoskeletal Proteins/chemistry ; Cytoskeletal Proteins/genetics ; Cytoskeletal Proteins/metabolism ; Cytoskeleton/metabolism ; Gene Knockdown Techniques ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Protein Domains ; Protein Folding ; Protein Stability ; Protein Structure, Quaternary ; Tight Junctions/metabolism ; Zonula Occludens-1 Protein/chemistry ; Zonula Occludens-1 Protein/genetics ; Zonula Occludens-1 Protein/metabolism
Chemical Substances	Cytoskeletal Proteins ; Phosphoproteins ; Zonula Occludens-1 Protein
Language	English
Publishing date	2022-03-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2022.101797
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Article ; Online: Mechanism of melanoma cells selective apoptosis induced by a photoactive NADPH analogue.

Rouaud, Florian / Boucher, Jean-Luc / Slama-Schwok, Anny / Rocchi, Stéphane

Oncotarget

2016 Volume 7, Issue 50, Page(s) 82804–82819

Abstract: Melanoma is one of the most lethal cancers when it reaches a metastatic stage. Despite the spectacular achievements of targeted therapies (BRAF inhibitors) or immuno-therapies (anti-CTLA4 or anti-PD1), most patients with melanoma will need additional ... ...

Abstract	Melanoma is one of the most lethal cancers when it reaches a metastatic stage. Despite the spectacular achievements of targeted therapies (BRAF inhibitors) or immuno-therapies (anti-CTLA4 or anti-PD1), most patients with melanoma will need additional treatments. Here we used a photoactive NADPH analogue called NS1 to induce cell death by inhibition of NADPH oxidases NOX in melanoma cells, including melanoma cells isolated from patients. In contrast, healthy melanocytes growth was unaffected by NS1 treatment.NS1 established an early Endoplasmic Reticulum stress by the early release of calcium mediated by (a) calcium-dependent redox-sensitive ion channel(s). These events initiated autophagy and apoptosis in all tested melanoma cells independently of their mutational status. The autophagy promoted by NS1 was incomplete. The autophagic flux was blocked at late stage events, consistent with the accumulation of p62, and a close localization of LC3 with NS1 associated with NS1 inhibition of NOX1 in autophagosomes. This hypothesis of a specific incomplete autophagy and apoptosis driven by NS1 was comforted by the use of siRNAs and pharmacological inhibitors blocking different processes. This study highlights the potential therapeutic interest of NS1 inducing cell death by triggering a selective ER stress and incomplete autophagy in melanoma cells harbouring wt and BRAF mutation.
MeSH term(s)	Animals ; Antineoplastic Agents/pharmacology ; Apoptosis/drug effects ; Autophagy/drug effects ; Calcium/metabolism ; Cell Line, Tumor ; Endoplasmic Reticulum Stress/drug effects ; Enzyme Inhibitors/pharmacology ; Humans ; Melanoma/drug therapy ; Melanoma/genetics ; Melanoma/metabolism ; Melanoma/pathology ; Mice ; Microtubule-Associated Proteins/metabolism ; Mutation ; NADP/analogs & derivatives ; NADP/pharmacology ; NADPH Oxidases/antagonists & inhibitors ; NADPH Oxidases/metabolism ; Proto-Oncogene Proteins B-raf/metabolism ; RAW 264.7 Cells ; RNA Interference ; Reactive Oxygen Species/metabolism ; Sequestosome-1 Protein/metabolism ; Signal Transduction/drug effects ; Skin Neoplasms/drug therapy ; Skin Neoplasms/genetics ; Skin Neoplasms/metabolism ; Skin Neoplasms/pathology ; Time Factors ; Transfection
Chemical Substances	Antineoplastic Agents ; Enzyme Inhibitors ; MAP1LC3A protein, human ; Microtubule-Associated Proteins ; Reactive Oxygen Species ; SQSTM1 protein, human ; Sequestosome-1 Protein ; NADP (53-59-8) ; NADPH Oxidases (EC 1.6.3.-) ; BRAF protein, human (EC 2.7.11.1) ; Proto-Oncogene Proteins B-raf (EC 2.7.11.1) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2016-09-30
Publishing country	United States
Document type	Journal Article
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.12651
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Article ; Online: The role of apical cell-cell junctions and associated cytoskeleton in mechanotransduction.

Sluysmans, Sophie / Vasileva, Ekaterina / Spadaro, Domenica / Shah, Jimit / Rouaud, Florian / Citi, Sandra

Biology of the cell

2017 Volume 109, Issue 4, Page(s) 139–161

Abstract: Tissues of multicellular organisms are characterised by several types of specialised cell-cell junctions. In vertebrate epithelia and endothelia, tight and adherens junctions (AJ) play critical roles in barrier and adhesion functions, and are connected ... ...

Abstract	Tissues of multicellular organisms are characterised by several types of specialised cell-cell junctions. In vertebrate epithelia and endothelia, tight and adherens junctions (AJ) play critical roles in barrier and adhesion functions, and are connected to the actin and microtubule cytoskeletons. The interaction between junctions and the cytoskeleton is crucial for tissue development and physiology, and is involved in the molecular mechanisms governing cell shape, motility, growth and signalling. The machineries which functionally connect tight and AJ to the cytoskeleton comprise proteins which either bind directly to cytoskeletal filaments, or function as adaptors for regulators of the assembly and function of the cytoskeleton. In the last two decades, specific cytoskeleton-associated junctional molecules have been implicated in mechanotransduction, revealing the existence of multimolecular complexes that can sense mechanical cues and translate them into adaptation to tensile forces and biochemical signals. Here, we summarise the current knowledge about the machineries that link tight and AJ to actin filaments and microtubules, and the molecular basis for mechanotransduction at epithelial and endothelial AJ.
MeSH term(s)	Animals ; Cadherins/metabolism ; Cell Polarity ; Cytoskeleton/metabolism ; Humans ; Intercellular Junctions/metabolism ; Mechanotransduction, Cellular/physiology
Chemical Substances	Cadherins
Language	English
Publishing date	2017-04
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	245745-3
ISSN	1768-322X ; 0399-0311 ; 0248-4900
ISSN (online)	1768-322X
ISSN	0399-0311 ; 0248-4900
DOI	10.1111/boc.201600075
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