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  1. Article ; Online: Paracingulin recruits CAMSAP3 to tight junctions and regulates microtubule and polarized epithelial cell organization.

    Flinois, Arielle / Méan, Isabelle / Mutero-Maeda, Annick / Guillemot, Laurent / Citi, Sandra

    Journal of cell science

    2023  Volume 137, Issue 5

    Abstract: Paracingulin (CGNL1) is recruited to tight junctions (TJs) by ZO-1 and to adherens junctions (AJs) by PLEKHA7. PLEKHA7 has been reported to bind to the microtubule minus-end-binding protein CAMSAP3, to tether microtubules to the AJs. Here, we show that ... ...

    Abstract Paracingulin (CGNL1) is recruited to tight junctions (TJs) by ZO-1 and to adherens junctions (AJs) by PLEKHA7. PLEKHA7 has been reported to bind to the microtubule minus-end-binding protein CAMSAP3, to tether microtubules to the AJs. Here, we show that knockout (KO) of CGNL1, but not of PLEKHA7, results in the loss of junctional CAMSAP3 and its redistribution into a cytoplasmic pool both in cultured epithelial cells in vitro and mouse intestinal epithelium in vivo. In agreement, GST pulldown analyses show that CGNL1, but not PLEKHA7, interacts strongly with CAMSAP3, and the interaction is mediated by their respective coiled-coil regions. Ultrastructure expansion microscopy shows that CAMSAP3-capped microtubules are tethered to junctions by the ZO-1-associated pool of CGNL1. The KO of CGNL1 results in disorganized cytoplasmic microtubules and irregular nuclei alignment in mouse intestinal epithelial cells, altered cyst morphogenesis in cultured kidney epithelial cells, and disrupted planar apical microtubules in mammary epithelial cells. Together, these results uncover new functions of CGNL1 in recruiting CAMSAP3 to junctions and regulating microtubule cytoskeleton organization and epithelial cell architecture.
    MeSH term(s) Animals ; Mice ; Adherens Junctions/metabolism ; Cytoplasm/metabolism ; Cytoskeletal Proteins/genetics ; Cytoskeletal Proteins/metabolism ; Epithelial Cells/metabolism ; Microtubule-Associated Proteins/metabolism ; Microtubules/metabolism ; Tight Junctions/metabolism
    Chemical Substances Camsap3 protein, mouse ; Cytoskeletal Proteins ; Microtubule-Associated Proteins ; Cgnl1 protein, mouse
    Language English
    Publishing date 2023-05-15
    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.260745
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1200: Show issues Location:
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  2. 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
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. 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
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. 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
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Uc I Zs.108: Show issues Location:
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  5. Article ; Online: LncRNA EPR controls epithelial proliferation by coordinating Cdkn1a transcription and mRNA decay response to TGF-β.

    Rossi, Martina / Bucci, Gabriele / Rizzotto, Dario / Bordo, Domenico / Marzi, Matteo J / Puppo, Margherita / Flinois, Arielle / Spadaro, Domenica / Citi, Sandra / Emionite, Laura / Cilli, Michele / Nicassio, Francesco / Inga, Alberto / Briata, Paola / Gherzi, Roberto

    Nature communications

    2019  Volume 10, Issue 1, Page(s) 1969

    Abstract: Long noncoding RNAs (lncRNAs) are emerging as regulators of fundamental biological processes. Here we report on the characterization of an intergenic lncRNA expressed in epithelial tissues which we termed EPR (Epithelial cell Program Regulator). EPR is ... ...

    Abstract Long noncoding RNAs (lncRNAs) are emerging as regulators of fundamental biological processes. Here we report on the characterization of an intergenic lncRNA expressed in epithelial tissues which we termed EPR (Epithelial cell Program Regulator). EPR is rapidly downregulated by TGF-β and its sustained expression largely reshapes the transcriptome, favors the acquisition of epithelial traits, and reduces cell proliferation in cultured mammary gland cells as well as in an animal model of orthotopic transplantation. EPR generates a small peptide that localizes at epithelial cell junctions but the RNA molecule per se accounts for the vast majority of EPR-induced gene expression changes. Mechanistically, EPR interacts with chromatin and regulates Cdkn1a gene expression by affecting both its transcription and mRNA decay through its association with SMAD3 and the mRNA decay-promoting factor KHSRP, respectively. We propose that EPR enables epithelial cells to control proliferation by modulating waves of gene expression in response to TGF-β.
    MeSH term(s) Animals ; Cell Proliferation/drug effects ; Cell Proliferation/genetics ; Cells, Cultured ; Cyclin-Dependent Kinase Inhibitor p21/genetics ; Cyclin-Dependent Kinase Inhibitor p21/metabolism ; Humans ; RNA Stability/genetics ; RNA, Long Noncoding/drug effects ; RNA, Long Noncoding/genetics ; Smad3 Protein/metabolism ; Transcriptome/genetics ; Transforming Growth Factor beta/pharmacology
    Chemical Substances Cyclin-Dependent Kinase Inhibitor p21 ; RNA, Long Noncoding ; Smad3 Protein ; Transforming Growth Factor beta
    Language English
    Publishing date 2019-04-29
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-019-09754-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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