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An adhesome comprising laminin, dystroglycan and myosin IIA is required during notochord development in Xenopus laevis.

Authors
  • Buisson, Nicolas
  • Sirour, Cathy
  • Moreau, Nicole
  • Denker, Elsa
  • Le Bouffant, Ronan
  • Goullancourt, Aline
  • Darribère, Thierry
  • Bello, Valérie
Type
Published Article
Journal
Development
Publisher
The Company of Biologists
Publication Date
Dec 01, 2014
Volume
141
Issue
23
Pages
4569–4579
Identifiers
DOI: 10.1242/dev.116103
PMID: 25359726
Source
Medline
Keywords
License
Unknown

Abstract

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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