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An atypical long signal peptide controls the translation efficiency and distribution of lipophorin receptors isoforms

AuthorsCuli, Joaquim ; Rodríguez-Vázquez, Míriam
Issue Date2013
Citation23rd European Drosophila Research Congress (2013)
AbstractDrosophila Lipophorin receptor 1 and 2 (Lpr1, Lpr2) are homologous to the human LDLR and they are involved in multiple processes, most notably lipid metabolism. Each receptor has two alternative promoters (P and D) that give rise to multiple isoforms (P- and D-isoforms) having strikingly different functions and tissue distributions. We found that these isoforms are subjected to differential post-transcriptional regulation when expressed in imaginal discs resulting in different translational efficiency, subcellular distribution and activity. We have mapped the protein domains required for this translational regulation to the signal peptide characteristic of D-isoforms. This signal peptide is predicted to be atypically long and thus, it may have additional functions besides targeting to the endoplasmic reticulum. We are currently studying how the signal peptide affects protein translation efficiency and function in multiple tissues where the lipophorin receptors have a critical role during lipid uptake.
DescriptionResumen del póster presentado al 23rd European Drosophila Research Congress, celebrado en Barcelona (España) del 16 al 19 de octubre de 2013.
Appears in Collections:(CABD) Comunicaciones congresos
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