Detecting phospholipase activity with the amphipathic lipid packing sensor motif of ArfGAP1
- Departamento de Química Biológica-Ranwel Caputto, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Haya de la Torre y Medina Allende S/n, Córdoba, X5000HUA (Argentina)
- Institut Curie, PSL Research University, CNRS, UMR 144, 26 Rue d’Ulm, 75248, Paris Cedex 05 (France)
Highlights: • The amphipathic lipid packing sensor (ALPS) motif of ArfGAP1 binds membranes of high curvature. • The activity of phospholipase A2, C and D on membranes generate lipids with high spontaneous curvature. • This in-situ phospholipase activity induces ALPS binding to membranes with small curvature. • We propose ALPS not only as a curvature sensor but also as a tool to monitor phospholipase activity. 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.
- OSTI ID:
- 23134155
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 505, Issue 1; Other Information: Copyright (c) 2018 Elsevier Inc. All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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