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  • Title: Detecting phospholipase activity with the amphipathic lipid packing sensor motif of ArfGAP1.
    Author: Quartino PY, Fidelio GD, Manneville JB, Goud B, Ambroggio EE.
    Journal: Biochem Biophys Res Commun; 2018 Oct 20; 505(1):290-294. PubMed ID: 30249399.
    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.
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