Structure-function analysis of the EGF-CFC family member Cripto identifies residues essential for nodal signalling (Articolo in rivista)

Type
Label
  • Structure-function analysis of the EGF-CFC family member Cripto identifies residues essential for nodal signalling (Articolo in rivista) (literal)
Anno
  • 2001-01-01T00:00:00+01:00 (literal)
Alternative label
  • Minchiotti G., Manco G., Parisi S., Lago C.T., Rosa F., Persico M.G. (2001)
    Structure-function analysis of the EGF-CFC family member Cripto identifies residues essential for nodal signalling
    in Development (Camb.)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Minchiotti G., Manco G., Parisi S., Lago C.T., Rosa F., Persico M.G. (literal)
Pagina inizio
  • 4501 (literal)
Pagina fine
  • 4510 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 128 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Titolo
  • Structure-function analysis of the EGF-CFC family member Cripto identifies residues essential for nodal signalling (literal)
Abstract
  • Cripto is the founding member of the family of EGF-CFC genes, a class of extracellular factors essential for early vertebrate development. In this study we show that injection of Cripto recombinant protein in mid to late zebrafish Maternal-Zygotic one-eyed pinhead (MZoep) blastulae was able to fully rescue the mutant phenotype, thus providing the first direct evidence that Cripto activity can be added extracellularly to recover oep-encoded function in zebrafish early embryos. Moreover, 15 point mutations and two deletion mutants were generated to assess in vivo their functional relevance by comparing the ability of cripto wild-type and mutant RNAs to rescue the zebrafish MZoep mutant. From this study we concluded that the EGF-CFC domain is sufficient for Cripto biological activity and identified ten point mutations with a functional defective phenotype, two of which, located in the EGF-like domain, correspond to loss-of-function mutations. Finally, we have developed a three-dimensional structural model of Cripto protein and used it as a guide to predict amino acid residues potentially implicated in protein-protein interaction. (literal)
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