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• W2893868943 abstract "The amphipathic lipid packing sensor (ALPS) motif of ArfGAP1 brings this GTPase activating protein to membranes of high curvature. Phospholipases are phospholipid-hydrolyzing enzymes that generate different lipid products that alter the lateral organization of membranes. Here, we evaluate by fluorescence microscopy how in-situ changes of membrane lipid composition driven by the activity of different phospholipases promotes the binding of ALPS. We show that the activity of phospholipase A2, phospholipase C and phospholipase D drastically enhances the binding of ALPS to the weakly-curved membrane of giant liposomes. Our results suggest that the enzymatic activity of phospholipases can modulate the ArfGAP1-mediated intracellular traffic and that amphiphilic peptides such as the ALPS motif can be used to study lipolytic activities at lipid membranes." @default.
• W2893868943 created "2018-10-05" @default.
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• W2893868943 date "2018-10-01" @default.
• W2893868943 modified "2023-09-30" @default.
• W2893868943 title "Detecting phospholipase activity with the amphipathic lipid packing sensor motif of ArfGAP1" @default.
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• W2893868943 doi "https://doi.org/10.1016/j.bbrc.2018.09.116" @default.
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