Etude du rôle des protéines de polarité Apico-Basale dans l' organisation des jonctions adhérentes

par Pauline Salis

Thèse de doctorat en Biologie du developpement

Sous la direction de André Le Bivic.

Le président du jury était Julien Royet.

Le jury était composé de Frederic Luton, Thomas Lecuit.

Les rapporteurs étaient Daniel St johnston, Roland Le borgne.


  • Résumé

    Epithelial tissues are composed of a sheet of adherent cells and are present in all metazoans. Their broad function is to compartmentalize tissues and enable the regulated exchange of nutrients and waste between the internal and external environments. To accomplish this function, cells require a specific organization: an apico-basal polarity that provides directionality and intercellular adhesion mediated by adherens junctions that hold cells together. How the epithelia architecture is initiated and maintained remains to be fully elucidated. Adherens junctions and the polarity proteins are functionally linked, as a loss of the main component of AJs: E-cadherin leads to a loss of apico-basal polarity, while disturbing apico-basal polarity results in a re-localization of E-Cadherin. Therefore is challenging to study either pathway in isolation.During my thesis I explored the role of Crumbs, a polarity protein, in the regulation of E-Cadherin in both AJ maturation and maintenance. During maturation of AJs in Drosophila embryo, I demonstrated for the first time by using quantitative high-resolution microscopy PALM that Crumbs regulates E-Cadherin clusters size and their homogenous distribution along the junction. In conclusion, my thesis work provides the first dissection of polarity proteins in E-Cadherin regulation apart from polarity pathways.

  • Titre traduit

    Role of apico-basal polarity proteins in E-Cadherin organization


  • Résumé

    Epithelial tissues are composed of a sheet of adherent cells and are present in all metazoans. Their broad function is to compartmentalize tissues and enable the regulated exchange of nutrients and waste between the internal and external environments. To accomplish this function, cells require a specific organization: an apico-basal polarity that provides directionality and intercellular adhesion mediated by adherens junctions that hold cells together. How the epithelia architecture is initiated and maintained remains to be fully elucidated. Adherens junctions and the polarity proteins are functionally linked, as a loss of the main component of AJs: E-cadherin leads to a loss of apico-basal polarity, while disturbing apico-basal polarity results in a re-localization of E-Cadherin. Therefore is challenging to study either pathway in isolation.During my thesis I explored the role of Crumbs, a polarity protein, in the regulation of E-Cadherin in both AJ maturation and maintenance. During maturation of AJs in Drosophila embryo, I demonstrated for the first time by using quantitative high-resolution microscopy PALM that Crumbs regulates E-Cadherin clusters size and their homogenous distribution along the junction. In conclusion, my thesis work provides the first dissection of polarity proteins in E-Cadherin regulation apart from polarity pathways.


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Informations

  • Détails : 1 vol. (137p.)
  • Annexes : bibliogr. p. 130-137

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  • Bibliothèque : Université Aix-Marseille (Marseille. Luminy). Service commun de la documentation. Bibliothèque de sciences.
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  • Bibliothèque : Université d'Aix-Marseille. Service commun de la documentation. Bibliothèque électronique.
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