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- W2891556949 abstract "Abstract The lipid distribution of plasma membranes of eukaryotic cells is asymmetric and phospholipid scramblases disrupt this asymmetry by mediating the rapid nonselective transport of lipids down their concentration gradients. As a result, phosphatidylserine is exposed to the outer leaflet of membrane, an important step in extracellular signaling networks controlling processes such as apoptosis, blood coagulation, membrane fusion and repair. Several members of the TMEM16 family have been identified as Ca 2+ -activated scramblases but the mechanisms underlying their Ca 2+ -dependent gating and their effects on the surrounding lipid bilayer remain poorly understood. Here we describe three high-resolution cryo-electron microscopy structures of a fungal scramblase from Aspergillus fumigatus , afTMEM16, reconstituted in lipid nanodiscs, revealing large Ca 2+ -dependent conformational changes of the protein as well as significant, function dependent membrane reorganization." @default.
- W2891556949 created "2018-09-27" @default.
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- W2891556949 date "2018-09-18" @default.
- W2891556949 modified "2023-09-24" @default.
- W2891556949 title "Cryo-EM structures reveal bilayer remodeling during Ca2+ activation of a TMEM16 scramblase" @default.
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- W2891556949 doi "https://doi.org/10.1101/420174" @default.
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