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An adhesome comprising laminin, dystroglycan and myosin IIA is required during notochord development in Xenopus laevis.
Buisson, Nicolas; Sirour, Cathy; Moreau, Nicole; Denker, Elsa; Le Bouffant, Ronan; Goullancourt, Aline; Darribère, Thierry; Bello, Valérie.
Afiliación
  • Buisson N; Sorbonne Universités, UPMC Univ. Paris 06, UMR CNRS 7622, Laboratoire de Biologie du Développement, 75252 Paris, Cedex 05, France.
  • Sirour C; Sorbonne Universités, UPMC Univ. Paris 06, UMR CNRS 7009, Observatoire Océanographique, Villefranche-sur-mer 06230, France.
  • Moreau N; Sorbonne Universités, UPMC Univ. Paris 06, UMR CNRS 7622, Laboratoire de Biologie du Développement, 75252 Paris, Cedex 05, France.
  • Denker E; Sars International Centre for Marine Molecular Biology, University of Bergen, Thormøhlensgt. 55, Bergen N-5008, Norway.
  • Le Bouffant R; Sorbonne Universités, UPMC Univ. Paris 06, UMR CNRS 7622, Laboratoire de Biologie du Développement, 75252 Paris, Cedex 05, France.
  • Goullancourt A; Sorbonne Universités, UPMC Univ. Paris 06, UMR CNRS 7622, Laboratoire de Biologie du Développement, 75252 Paris, Cedex 05, France.
  • Darribère T; Sorbonne Universités, UPMC Univ. Paris 06, UMR CNRS 7622, Laboratoire de Biologie du Développement, 75252 Paris, Cedex 05, France thierry.darribere@upmc.fr valerie.bello@snv.jussieu.fr.
  • Bello V; Sorbonne Universités, UPMC Univ. Paris 06, UMR CNRS 7622, Laboratoire de Biologie du Développement, 75252 Paris, Cedex 05, France thierry.darribere@upmc.fr valerie.bello@snv.jussieu.fr.
Development ; 141(23): 4569-79, 2014 Dec.
Article en En | MEDLINE | ID: mdl-25359726
Dystroglycan (Dg) is a transmembrane receptor for laminin that must be expressed at the right time and place in order to be involved in notochord morphogenesis. The function of Dg was examined in Xenopus laevis embryos by knockdown of Dg and overexpression and replacement of the endogenous Dg with a mutated form of the protein. This analysis revealed that Dg is required for correct laminin assembly, for cell polarization during mediolateral intercalation and for proper differentiation of vacuoles. Using mutations in the cytoplasmic domain, we identified two sites that are involved in cell polarization and are required for mediolateral cell intercalation, and a site that is required for vacuolation. Furthermore, using a proteomic analysis, the cytoskeletal non-muscle myosin IIA has been identified for the first time as a molecular link between the Dg-cytoplasmic domain and cortical actin. The data allowed us to identify the adhesome laminin-Dg-myosin IIA as being required to maintain the cortical actin cytoskeleton network during vacuolation, which is crucial to maintain the shape of notochordal cells.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Vacuolas / Xenopus laevis / Laminina / Miosina Tipo IIA no Muscular / Organogénesis / Distroglicanos / Notocorda Límite: Animals Idioma: En Revista: Development Asunto de la revista: BIOLOGIA / EMBRIOLOGIA Año: 2014 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Vacuolas / Xenopus laevis / Laminina / Miosina Tipo IIA no Muscular / Organogénesis / Distroglicanos / Notocorda Límite: Animals Idioma: En Revista: Development Asunto de la revista: BIOLOGIA / EMBRIOLOGIA Año: 2014 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Reino Unido