spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

This Article
Right arrow Figures Only
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Andrenacci, D.
Right arrow Articles by Gargiulo, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Andrenacci, D.
Right arrow Articles by Gargiulo, G.
Journal of Cell Science 114, 2819-2829 (2001)
© 2001 The Company of Biologists Limited

RESEARCH ARTICLE

Specific domains drive VM32E protein distribution and integration in Drosophila eggshell layers

Davide Andrenacci1, Filippo M. Cernilogar1, Carlo Taddei1, Deborah Rotoli2,*, Valeria Cavaliere1, Franco Graziani2 and Giuseppe Gargiulo1,{ddagger}

1 Dipartimento di Biologia Evoluzionistica Sperimentale, Via Selmi 3, 40126 Bologna, Italy
2 Istituto Internazionale di Genetica e Biofisica; Via Marconi 10, 80125 Napoli, Italy
* Present address: Centro di Oncologia Sperimentale, CNR, Via Pansini 2 Napoli, Italy
{ddagger} Author for correspondence (e-mail: gargiulo_g{at}biblio.cib.unibo.it )

Accepted April 27, 2001

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 vitelline membrane proteins.

Key words: Oogenesis, Follicle cells, Eggshell, Vitelline membrane, Endochorion




This article has been cited by other articles:


Home page
 Mol Biol EvolHome page
S. Jagadeeshan and R. S. Singh
Rapid Evolution of Outer Egg Membrane Proteins in the Drosophila melanogaster Subgroup: A Case of Ecologically Driven Evolution of Female Reproductive Traits
Mol. Biol. Evol., April 1, 2007; 24(4): 929 - 938.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 2001