Specific domains drive VM32E protein distribution and integration in Drosophila eggshell layers. (Articolo in rivista)

Type
Label
  • Specific domains drive VM32E protein distribution and integration in Drosophila eggshell layers. (Articolo in rivista) (literal)
Anno
  • 2001-01-01T00:00:00+01:00 (literal)
Alternative label
  • Andrenacci D, Cernilogar FM, Taddel C, Rotoli D, Cavaliere V, Graziani F, Gargiulo G (2001)
    Specific domains drive VM32E protein distribution and integration in Drosophila eggshell layers.
    in Journal of cell science
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Andrenacci D, Cernilogar FM, Taddel C, Rotoli D, Cavaliere V, Graziani F, Gargiulo G (literal)
Pagina inizio
  • 2819 (literal)
Pagina fine
  • 2829 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 114 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#descrizioneSinteticaDelProdotto
  • In questo lavoro viene dimostrato che il prodotto del gene VM32E viene sintetizzato solo nelle cellule follicolari laterali e successivamente trasportato al polo anteriore e posteriore della camera ovarica. (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Dipartimento di Biologia Evoluzionistica Sperimentale, Bologna, Italy. Istituto di Genetica e Biofisica-ABT CNR Napoli (literal)
Titolo
  • Specific domains drive VM32E protein distribution and integration in Drosophila eggshell layers. (literal)
Abstract
  • A study was made of the localization and assembly of the VM32E protein, a putative vitelline membrane component of the Drosophila eggshell. The results highlight some unique features of this protein compared with the other proteins of the same gene family. At the time of its synthesis (stage 10), the VM32E protein is not detectable in polar follicle cells. However, it is able to move in the extracellular space around the oocyte and, by stage 11 is uniformly distributed in the vitelline membrane. During the terminal stages of oogenesis the VM32E protein is partially released from the vitelline membrane and becomes localized in the endochorion layer also. By analyzing transgenic flies carrying variously truncated VM32E proteins, we could identify the protein domains required for the proper assembly of the VM32E protein in the eggshell. The highly conserved vitelline membrane domain is implicated in the early interactions with other components and is required for cross-linking VM32E protein in the vitelline membrane. The terminal carboxylic domain is necessary for localization to the endochorion layer. Protein with the C-end domain deleted is localized solely to the vitelline membrane and cross-linked only in laid eggs, as occurs for the other (literal)
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