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4 results on '"Dynamique de l’organisation intra-cellulaire"'

1. Caveolae promote successful abscission by controlling intercellular bridge tension during cytokinesis

Author

Virginia Andrade, Jian Bai, Neetu Gupta-Rossi, Ana Joaquina Jimenez, Cédric Delevoye, Christophe Lamaze, Arnaud Echard, Trafic membranaire et Division cellulaire - Membrane Traffic and Cell Division, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), Sorbonne Université (SU), Dynamique de l’organisation intra-cellulaire, Biologie Cellulaire et Cancer, Institut Curie [Paris]-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut Curie [Paris]-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), BioImaging Cell and Tissue Core Facility (PICT-IBiSA), Institut Curie [Paris], Structure et compartimentation membranaire, Compartimentation et dynamique cellulaires (CDC), Chimie biologique des membranes et ciblage thérapeutique (CBMCT - UMR 3666 / U1143), Université Paris Descartes - Paris 5 (UPD5)-Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), This work was supported by Institut Pasteur (A.E.), CNRS (A.E.), ANR Cytosign, ANR SeptScort (A.E.), ANR MOTICAV (C.L.), ANR CAV-SM (C.L.), Fondation pour le Recherche Médicale: Recherche soutenue par la FRM EQU202103012627 (A.E.), French National Research Agency through the 'Investments for the Future' program, France-BioImaging, ANR-10-INSB-04 (C.D.), Cell and Tissue Imaging core facility (PICT-IBiSA), member of the France-BioImaging national research infrastructure, supported by the Labex Cell(n)Scale (ANR-10-LBX-0038) part of the IDEX PSL (ANR-10-IDEX-0001-02 PSL) (C.D. and C.L.), Doctoral School Complexité du Vivant ED515, contrat n° 2828/2017 (V.A.), La Ligue Contre le Cancer (4ème année de thèse) (V.A.), Pasteur-Paris University (PPU) international PhD program (J.B.), Fondation ARC pour la recherche sur le cancer (DOC20180507410) (J.B.), Programme Labellisé PGA1-RF20170205456 (C.L.), and CEFIPRA, project 6301-1., ANR-16-CE13-0004,CYTOSIGN,Polarité épithéliale et signalisation au cours de la cytodiérèse des cellules animales(2016), ANR-20-CE11-0014,SeptScort,Interaction spatiale et fonctionnelle entre septines et Escrt pendant la cytocinèse: une approche multi-échelle(2020), ANR-17-CE13-0020,MOTICAV,Cavéoles et Tension Membranaire dans la Migration Cellulaire(2017), ANR-20-CE13-0002,CAV-SM,Un rôle nouveau de la cavéoline dans le transport de la sphingomyéline à la membrane plasmique(2020), ANR-10-INBS-0004,France-BioImaging,Développment d'une infrastructure française distribuée coordonnée(2010), ANR-10-IDEX-0001,PSL,Paris Sciences et Lettres(2010), Collège Doctoral, Institut Curie [Paris]-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), and Agence Nationale de la Recherche: CytosignAgence Nationale de la Recherche: SeptScortAgence Nationale de la Recherche: ANR-10-INSB-04Agence Nationale de la Recherche: ANR-10-LBX-0038Agence Nationale de la Recherche: ANR-10-IDEX-0001-02 PSLInstitut PasteurFondation ARC pour la Recherche sur le Cancer: DOC20180507410La Ligue Contre Le CancerDoctoral School Complexité du Vivant ED515: 2828/2017CNRSPasteur-Paris University (PPU) international PhD program

Subjects
Multidisciplinary, [SDV]Life Sciences [q-bio], macromolecular substances
Abstract

During cytokinesis, the intercellular bridge (ICB) connecting the daughter cells experiences pulling forces, which delay abscission by preventing the assembly of the ESCRT scission machinery. Abscission is thus triggered by tension release, but how ICB tension is controlled is unknown. Here, we report that caveolae, which are known to control membrane tension upon mechanical stress in interphase cells, are located at the midbody, at the abscission site and at the ICB/cell interface in dividing cells. Functionally, the loss of caveolae delays ESCRT-III recruitment during cytokinesis and impairs abscission. This is the consequence of a 2-fold increase of ICB tension measured by laser ablation, associated with a local increase in myosin II activity at the ICB/cell interface. We thus propose that caveolae buffer membrane tension and limit contractibility at the ICB to promote ESCRT-III assembly and cytokinetic abscission. Altogether, this work reveals an unexpected connection between caveolae and the ESCRT machinery and the first role of caveolae in cell division.TEASERCaveolae limit the tension in the intercellular bridge during cytokinesis to enable ESCRT-III assembly and successful abscission.

Published
2022
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2. Isoformes de Cdc42 : localisation, fonctions et régulation

Author

Ravichandran, Yamini, Polarité cellulaire, Migration et Cancer - Cell Polarity, Migration and Cancer, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Dynamique de l’organisation intra-cellulaire, Biologie Cellulaire et Cancer, Institut Curie [Paris]-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut Curie [Paris]-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Sorbonne Université, Jean-Baptiste Manneville, and Sandrine Étienne-Manneville

Subjects
Cellular polarity, Golgi-apparatus, Subcellular localization, Polarité cellulaire, Cdc42 isoformes, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Maladies rares, Cdc42 isoforms, Rare diseases, Localisation intracellulaire, Régulation de Cdc42, Cell migration, Regulation of Cdc42, Migration cellulaire
Abstract

Mutations in proteins cause diverse developmental disorders, particularly for individuals with rare diseases or for whom a unifying clinical diagnosis is unknown. Cdc42 is one such protein; vital for establishing cell polarity, a crucial step in many biological processes such as cell migration, division and immune responses. Not surprisingly, mutations in Cdc42 cause a range of diseases such as growth dysregulation, facial dysmorphism and neurodevelopmental, immunological, and hematological abnormalities. In vertebrates there are two isoforms of Cdc42. The first being the ubiquitous isoform, has almost exclusively been studied and the role of the second isoform, being the brain isoform, is largely unknown. We have shown that the two isoforms are localized differently in cells. The ubiquitous isoform is mostly found in the cell cytoplasm and at the plasma membrane, while the Brain isoform localizes at the Golgi apparatus and on intracellular vesicles. We have also shown that the two isoforms carry out different functions during cell migration, suggesting that the differences between these two isoforms which only differs by the last 10 amino acids are responsible for their distinct localisation and function. Interestingly, a mutation in the C-ter sequence of Cdc42 ubiquitous isoform alters Cdc42 localisation and causes a generalized pustular psoriasis disease. Two main objectives have been studied in this project 1) the impact of the last amino acids of the protein in Cdc42 localization; and 2) new regulatory mechanisms of Cdc42 responsible for its intracellular localization. These findings will bring a better understanding of pathologies related to Cdc42 mutations.; Les mutations sont responsables de diverses pathologies du développement, en particulier chez les patients atteints de maladies rares ou pour lesquels il n’y a pas de diagnostic clinique clair. Cdc42 est une protéine clé pour la polarité cellulaire, une étape cruciale de nombreux processus cellulaires, comme la migration cellulaire, la division cellulaire ou la réponse immunitaire. Les mutations de Cdc42 entrainent une variété de pathologies, par exemple des dérégulations de la croissance ou de la morphologie faciale ainsi que des anomalies immunologiques, hématologiques et du développement neuronal. Les fonctions de Cdc42 reposent en grande partie sur la localisation de cette protéine dans la cellule. La comparaison des différentes formes de Cdc42 et de certaines formes mutantes montrent que les derniers acides aminés de la protéine jouent un rôle clé dans sa localisation et donc dans sa fonction. Nous avons centré notre étude sur l’identification : 1) des acides aminés essentiels à la localisation de la protéine ; et 2) de nouveaux mécanismes de régulation de Cdc42 responsables de sa localisation intracellulaire. Nous avons aussi montré que les deux isoformes jouent des rôles différents au cours de la migration cellulaire. Ce travail devrait nous permettre de mieux comprendre les pathologies liées aux mutations de Cdc42.

Published
2020

3. Targeting CCR5 trafficking to inhibit HIV-1 infection

Author

Anne Brelot, Elaine Del Nery, Yuko Fukata, Gaelle Boncompain, Masaki Fukata, Isabelle Staropoli, Sarah Tessier, Floriane Herit, Pierre Gestraud, Florence Niedergang, Franck Perez, Aurianne Lescure, Université Paris sciences et lettres (PSL), Dynamique de l’organisation intra-cellulaire, Biologie Cellulaire et Cancer, Institut Curie [Paris]-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut Curie [Paris]-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Institut Cochin (IC UM3 (UMR 8104 / U1016)), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de criblage à haute teneur en biophénic [Institut Curie] (Biophenics High-Content Screening Laboratory), Institut Curie [Paris]-Université Paris sciences et lettres (PSL), Cancer et génome: Bioinformatique, biostatistiques et épidémiologie d'un système complexe, Mines Paris - PSL (École nationale supérieure des mines de Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Pathogénie Virale - Viral Pathogenesis, Institut Pasteur [Paris] (IP)-Institut National de la Santé et de la Recherche Médicale (INSERM), Division of Membrane Physiology, Department of Molecular and Cellular Physiology [Okazaki], National Institute for Physiological Sciences-National Institutes of Natural Sciences [Tokyo] (NINS), We acknowledge the Cell and Tissue Imaging Facility (PICT-IBiSA), Institut Curie, a member of the French National Research Infrastructure, France-BioImaging (ANR10-INBS-04). This work was supported by grants from CNRS, INSERM, Université Paris Descartes, Agence Nationale de la Recherche (2011 BSV3 025 02), and Agence Nationale de Recherches sur le Sida et les Hépatites (ANRS, AO2012-2) to A.B., F.P., and F.N., and Fondation pour la Recherche Médicale (FRM DEQ20130326518) to F.N. This work has received support under the 'Investissements d’Avenir' program launched by the French government and implemented by ANR with the references ANR-10-LABX-62-IBEID and ANR-10-IDEX-0001-02 PSL, ANR-10-INBS-0004,France-BioImaging,Développment d'une infrastructure française distribuée coordonnée(2010), ANR-10-LABX-0062,IBEID,Integrative Biology of Emerging Infectious Diseases(2010), ANR-10-IDEX-0001,PSL,Paris Sciences et Lettres(2010), PSL Research University (PSL), Institut Curie-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut Curie-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Institut Curie-PSL Research University Paris, Cancer et génôme: Bioinformatique, biostatistiques et épidémiologie d'un système complexe, MINES ParisTech - École nationale supérieure des mines de Paris-Institut Curie-Institut National de la Santé et de la Recherche Médicale (INSERM), Pathogénie Virale, Institut Pasteur [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), ANR-10-INBS-04-01/10-INBS-0004,France-BioImaging,Développment d'une infrastructure française distribuée coordonnée(2010), ANR-10-LABX-62-IBEID,IBEID,Laboratoire d'Excellence 'Integrative Biology of Emerging Infectious Diseases'(2010), ANR-10-IDEX-0001-02/10-IDEX-0001,PSL,Paris Sciences et Lettres(2010), Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut Curie [Paris]-MINES ParisTech - École nationale supérieure des mines de Paris, and Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)

Subjects
CCR1, Receptors, CXCR4, Receptors, CCR5, Cell, Receptors, CCR1, HIV Infections, CXCR4, Cell Line, 03 medical and health sciences, 0302 clinical medicine, Palmitoylation, [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases, Cell Line, Tumor, medicine, Humans, Amino Acid Sequence, 030212 general & internal medicine, Receptor, Research Articles, Secretory pathway, 030304 developmental biology, 0303 health sciences, Secretory Pathway, Multidisciplinary, Chemistry, Macrophages, HEK 293 cells, SciAdv r-articles, virus diseases, Cell Biology, respiratory system, 3. Good health, Transport protein, Cell biology, Protein Transport, HEK293 Cells, medicine.anatomical_structure, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, HIV-1, human activities, HeLa Cells, Research Article
Abstract

The diversity of secretory routes enabled the identification of specific inhibitors of CCR5 transport and HIV-1 infection., Using a cell-based assay monitoring differential protein transport in the secretory pathway coupled to high-content screening, we have identified three molecules that specifically reduce the delivery of the major co-receptor for HIV-1, CCR5, to the plasma membrane. They have no effect on the closely related receptors CCR1 and CXCR4. These molecules are also potent in primary macrophages as they markedly decrease HIV entry. At the molecular level, two of these molecules inhibit the critical palmitoylation of CCR5 and thereby block CCR5 in the early secretory pathway. Our results open a clear therapeutics avenue based on trafficking control and demonstrate that preventing HIV infection can be performed at the level of its receptor delivery.

Published
2019
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4. Dendritic Cells Require TMEM176A/B Ion Channels for Optimal MHC Class II Antigen Presentation to Naive CD4 + T Cells.

Author

Lancien M, Bienvenu G, Salle S, Gueno L, Feyeux M, Merieau E, Remy S, Even A, Moreau A, Molle A, Fourgeux C, Coulon F, Beriou G, Bouchet-Delbos L, Chiffoleau E, Kirstetter P, Chan S, Kerfoot SM, Abdu Rahiman S, De Simone V, Matteoli G, Boncompain G, Perez F, Josien R, Poschmann J, Cuturi MC, and Louvet C

Subjects
Animals, Endosomes immunology, Female, Genes, MHC Class II immunology, Golgi Apparatus immunology, Immunity, Innate immunology, Intestinal Mucosa immunology, Ion Channels immunology, Lymphocytes immunology, Lysosomes immunology, Male, Mice, Mice, Inbred C57BL, Mice, Knockout, Th17 Cells immunology, Tretinoin immunology, Antigen Presentation immunology, CD4-Positive T-Lymphocytes immunology, Dendritic Cells immunology, Histocompatibility Antigens Class II immunology, Membrane Proteins immunology
Abstract

Intracellular ion fluxes emerge as critical actors of immunoregulation but still remain poorly explored. In this study, we investigated the role of the redundant cation channels TMEM176A and TMEM176B (TMEM176A/B) in retinoic acid-related orphan receptor γt + cells and conventional dendritic cells (DCs) using germline and conditional double knockout mice. Although Tmem176a/b appeared surprisingly dispensable for the protective function of Th17 and group 3 innate lymphoid cells in the intestinal mucosa, we found that they were required in conventional DCs for optimal Ag processing and presentation to CD4 + T cells. Using a real-time imaging method, we show that TMEM176A/B accumulate in dynamic post-Golgi vesicles preferentially linked to the late endolysosomal system and strongly colocalize with HLA-DM. Taken together, our results suggest that TMEM176A/B ion channels play a direct role in the MHC class II compartment of DCs for the fine regulation of Ag presentation and naive CD4 + T cell priming., (Copyright © 2021 by The American Association of Immunologists, Inc.)

Published
2021
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