drosophila lipophorin receptors mediate the uptake of neutral lipids in oocytes and imaginal disc cells by an endocytosis-independent mechanism果蝇lipophorin受体调节的中性脂质吸收endocytosis-independent卵母细胞和成虫盘细胞的机制.pdfVIP
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drosophila lipophorin receptors mediate the uptake of neutral lipids in oocytes and imaginal disc cells by an endocytosis-independent mechanism果蝇lipophorin受体调节的中性脂质吸收endocytosis-independent卵母细胞和成虫盘细胞的机制
Drosophila Lipophorin Receptors Mediate the Uptake of
Neutral Lipids in Oocytes and Imaginal Disc Cells by an
Endocytosis-Independent Mechanism
Esmeralda Parra-Peralbo, Joaquim Culi*
´
Centro Andaluz de Biologıa del Desarrollo (CSIC-UPO), Universidad Pablo de Olavide, Sevilla, Spain
Abstract
Lipids are constantly shuttled through the body to redistribute energy and metabolites between sites of absorption,
storage, and catabolism in a complex homeostatic equilibrium. In Drosophila, lipids are transported through the
hemolymph in the form of lipoprotein particles, known as lipophorins. The mechanisms by which cells interact with
circulating lipophorins and acquire their lipidic cargo are poorly understood. We have found that lipophorin receptor 1 and 2
(lpr1 and lpr2), two partially redundant genes belonging to the Low Density Lipoprotein Receptor (LDLR) family, are
essential for the efficient uptake and accumulation of neutral lipids by oocytes and cells of the imaginal discs. Females
lacking the lpr2 gene lay eggs with low lipid content and have reduced fertility, revealing a central role for lpr2 in mediating
Drosophila vitellogenesis. lpr1 and lpr2 are transcribed into multiple isoforms. Interestingly, only a subset of these isoforms
containing a particular LDLR type A module mediate neutral lipid uptake. Expression of these isoforms induces the
extracellular stabilization of lipophorins. Furthermore, our data indicate that endocytosis of the lipophorin receptors is not
required to mediate the uptake of neutral lipids. These findings suggest a model where lipophorin receptors promote the
extracellular lipolysis of lipophorins. This model is reminiscent of the lipolytic processing of triglyceride-rich lipoprotein
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