@misc{49341, type = "Article", year = "2014", title = "Modelization of the regulation of protein synthesis following fertilization in sea urchin shows requirement of two processes: a destabilization of elF4E:4E-BP complex and a great stimulation of the 4E-BP-degradation mechanism, both rapamycin-sensitive", journal = "Frontiers In Genetics", editor = "Frontiers Media Sa", volume = "5", number = "117", pages = "1-10", author = "Laurent Sebastien, Richard Adrien, Mulner-Lorillon Odile, Morales Julia, Flament Didier, Glippa Virginie, Bourdon Jeremie, Gosselin Pauline, Siegel Anne, Cormier Patrick, Belle Robert", url = "https://archimer.ifremer.fr/doc/00382/49341/", organization = "", address = "FRANCE", doi = "https://doi.org/10.3389/fgene.2014.00117", abstract = "
Fertilization of sea urchin eggs involves an increase in protein synthesis associated with a decrease in the amount of the translation initiation inhibitor 4E-BP A highly simple reaction model for the regulation of protein synthesis was built and was used to simulate the physiological changes in the total 4E-BP amount observed during time after fertilization. Our study evidenced that two changes occurring at fertilization are necessary to fit with experimental data. The first change was an 8-fold increase in the dissociation parameter (koffi) of the elF4E:4E-BP complex. The second was an important 32.5-fold activation of the degradation mechanism of the protein 4E-BP Additionally, the changes in both processes should occur in 5 min time interval post-fertilization. To validate the model, we checked that the kinetic of the predicted 4.2-fold increase of elF4E:e1F4G complex concentration at fertilization matched the increase of protein synthesis experimentally observed after fertilization (6.6-fold, SD = 2.3, n = 8). The minimal model was also used to simulate changes observed after fertilization in the presence of rapamycin, a FRAP/mTOR inhibitor. The model showed that the elF4E:4E-BP complex destabilization was impacted and surprisingly, that the mechanism of 4E-BP degradation was also strongly affected, therefore suggesting that both processes are controlled by the protein kinase FRAP/mTOR.
", key = "" }