Coordinatore | INSTITUTO DE TECNOLOGIA QUIMICA E BIOLOGICA - UNIVERSIDADE NOVA DE LISBOA
Organization address
address: "Avenida da Republica, Estacao Agronomica Nacional" contact info |
Nazionalità Coordinatore | Portugal [PT] |
Totale costo | 100˙000 € |
EC contributo | 100˙000 € |
Programma | FP7-PEOPLE
Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013) |
Code Call | FP7-PEOPLE-IRG-2008 |
Funding Scheme | MC-IRG |
Anno di inizio | 2008 |
Periodo (anno-mese-giorno) | 2008-12-01 - 2014-04-01 |
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INSTITUTO DE TECNOLOGIA QUIMICA E BIOLOGICA - UNIVERSIDADE NOVA DE LISBOA
Organization address
address: "Avenida da Republica, Estacao Agronomica Nacional" contact info |
PT (OEIRAS) | coordinator | 0.00 |
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'The endoplasmic reticulum (ER) is the cell organelle where secretory and membrane proteins are synthesized and folded. The presence of unfolded/misfolded proteins in the ER causes stress to the cell (“ER stress”) and activates the Unfolded Protein Response (UPR), a cellular response to restore homeostasis in the ER. The presence of misfolded proteins and activation of the UPR have been connected with many diseases and pathological conditions. My goal is to elucidate the molecular mechanisms that regulate neuronal degeneration and cell death induced by ER strees, using Drosophila melanogaster as a model system. To achieve this goal, I propose the following specific aims: 1. Analysis of the molecular mechanisms required for induction of cell death in the context of ER stress. 2. The mechanism of induction of cell death by Xbp1spliced 3. Developmental role of the UPR during photoreceptor differentiation.'
Proteins that are not folded properly are connected with many diseases. An EU-funded project has investigated one such example, retinitis pigmentosa (RP), a major cause of blindness.