A new role for the architecture of microvillar actin bundles in apical retention of membrane proteins
| Autor: | Sylvie Robine, Edith Brot-Laroche, Delphine Delacour, Daniel Louvard, Francisco Rivero, Céline Revenu, Ilse Hurbain, Damarys Loew, Fatima El-Marjou, Florent Ubelmann, Florent Dingli, Jules Gilet |
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| Přispěvatelé: | Compartimentation et dynamique cellulaires ( CDC ), Centre National de la Recherche Scientifique ( CNRS ) -INSTITUT CURIE-Université Pierre et Marie Curie - Paris 6 ( UPMC ), BioImaging Cell and Tissue Core Facility ( PICT-IBiSA ), INSTITUT CURIE, Laboratoire de Spectrométrie de Masse Protéomique, Institut Jacques Monod ( IJM ), Université Paris Diderot - Paris 7 ( UPD7 ) -Centre National de la Recherche Scientifique ( CNRS ), Centre de Recherche des Cordeliers ( CRC (UMR_S 872) ), Université Pierre et Marie Curie - Paris 6 ( UPMC ) -Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Centre for Biomedical Research, University of Hull, University of Hull, CNRS, Association pour la Recherche contre le Cancer, Ministère de la Recherche et de la Technologie, Fondation pour la Recherche Médicale, Cancéropôle Ile-de-France, INCA, Compartimentation et dynamique cellulaires (CDC), Centre National de la Recherche Scientifique (CNRS)-Institut Curie [Paris]-Université Pierre et Marie Curie - Paris 6 (UPMC), BioImaging Cell and Tissue Core Facility (PICT-IBiSA), Institut Curie [Paris], Institut Jacques Monod (IJM (UMR_7592)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherche des Cordeliers (CRC (UMR_S 872)), Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut Curie [Paris]-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut Curie-Université Pierre et Marie Curie - Paris 6 (UPMC), Institut Curie |
| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
MESH: Microvilli
Endocytic cycle MESH: Membrane Glycoproteins MESH : Actins MESH : Membrane Glycoproteins MESH: Mice Knockout MESH: Myosin Heavy Chains Mice MESH: Protein Structure Tertiary MESH: Enterocytes 0302 clinical medicine Myosin MESH: Animals Cytoskeleton Mice Knockout 0303 health sciences Membrane Glycoproteins Microvilli MESH : Myosin Heavy Chains Microfilament Proteins Microfilament Protein Articles Cell biology MESH : Enterocytes MESH : Microscopy Electron Transmission MESH: Microscopy Electron Transmission Villin MESH : Protein Structure Tertiary MESH : Microfilament Proteins Morphogenesis macromolecular substances [ SDV.BBM.BM ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology Biology MESH: Actins 03 medical and health sciences MESH: Microfilament Proteins Microscopy Electron Transmission MESH : Mice Animals Molecular Biology MESH: Mice Actin 030304 developmental biology Myosin Heavy Chains [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology Cell Biology Actins Protein Structure Tertiary Membrane glycoproteins Enterocytes MESH : Microvilli Membrane protein biology.protein MESH : Mice Knockout sense organs MESH : Animals 030217 neurology & neurosurgery |
| Zdroj: | Molecular Biology of the Cell Molecular Biology of the Cell, American Society for Cell Biology, 2012, 23 (2), pp.324-36. 〈10.1091/mbc.E11-09-0765〉 Molecular Biology of the Cell, American Society for Cell Biology, 2012, 23 (2), pp.324-36. ⟨10.1091/mbc.E11-09-0765⟩ Molecular Biology of the Cell, 2012, 23 (2), pp.324-36. ⟨10.1091/mbc.E11-09-0765⟩ |
| ISSN: | 1059-1524 1939-4586 |
| DOI: | 10.1091/mbc.E11-09-0765〉 |
| Popis: | The bundled architecture of actin filaments is not needed for intestinal microvillar morphogenesis, as shown in knockout mice devoid of microvillar actin-bundling proteins. This architecture is essential for the apical anchorage of digestive proteins, probably via the recruitment of key players in apical retention, such as myosin-1a, and, as a result, for intestinal physiology. Actin-bundling proteins are identified as key players in the morphogenesis of thin membrane protrusions. Until now, functional redundancy among the actin-bundling proteins villin, espin, and plastin-1 has prevented definitive conclusions regarding their role in intestinal microvilli. We report that triple knockout mice lacking these microvillar actin-bundling proteins suffer from growth delay but surprisingly still develop microvilli. However, the microvillar actin filaments are sparse and lack the characteristic organization of bundles. This correlates with a highly inefficient apical retention of enzymes and transporters that accumulate in subapical endocytic compartments. Myosin-1a, a motor involved in the anchorage of membrane proteins in microvilli, is also mislocalized. These findings illustrate, in vivo, a precise role for local actin filament architecture in the stabilization of apical cargoes into microvilli. Hence, the function of actin-bundling proteins is not to enable microvillar protrusion, as has been assumed, but to confer the appropriate actin organization for the apical retention of proteins essential for normal intestinal physiology. |
| Databáze: | OpenAIRE |
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