Homeostasis of cellular membranes is maintained by fine-tuning their lipid composition. Yeast lipid transporter Osh6, belonging to the oxysterol-binding protein-related proteins family, was found to participate in the transport of phosphatidylserine (PS). PS synthesized in the endoplasmic reticulum is delivered to the plasma membrane, where it is exchanged for phosphatidylinositol 4-phosphate (PI4P). PI4P provides the driving force for the directed PS transport against its concentration gradient. In this study, we employed an in vitro approach to reconstitute the transport process into the minimalistic system of large unilamellar vesicles to reveal its fundamental biophysical determinants. Our study draws a comprehensive portrait of the interplay between the structure and dynamics of Osh6, the carried cargo lipid, and the physical properties of the involved membranes, with particular attention to the presence of charged lipids and to membrane fluidity. Specifically, we address the role of the cargo lipid, which, by occupying the transporter, imposes changes in its dynamics and, consequently, predisposes the cargo to disembark in the correct target membrane.

• MeSH
• biologický transport MeSH
• buněčná membrána * metabolismus   MeSH
• fluidita membrány MeSH
• fosfatidylinositolfosfáty metabolismus   MeSH
• fosfatidylseriny metabolismus   MeSH
• proteiny vázající oxysterol MeSH
• Saccharomyces cerevisiae - proteiny * metabolismus   genetika   MeSH
• Saccharomyces cerevisiae metabolismus   MeSH
• steroidní receptory metabolismus   MeSH
• unilamelární lipozómy metabolismus   MeSH
• Publikační typ
• časopisecké články MeSH
• Názvy látek
• fosfatidylinositolfosfáty MeSH
• fosfatidylseriny MeSH
• phosphatidylinositol 4-phosphate MeSH Prohlížeč
• proteiny vázající oxysterol MeSH
• Saccharomyces cerevisiae - proteiny * MeSH
• steroidní receptory MeSH
• unilamelární lipozómy MeSH