Phospholipase A2 promotes raft budding and fission from giant liposomes

• DOI: 10.1016/j.chemphyslip.2003.11.005
• Publication Date: 2004-01-23T10:18:16Z
• Authors: Galya Staneva; Miglena I. Angelova; Kamen Koumanov
• Keywords: 0301 basic medicine; Phospholipases A2; 03 medical and health sciences; Membrane Microdomains; Microscopy, Video; Microinjections; Liposomes; Temperature; Golgi Apparatus; Phospholipases A

Cellular processes involving membrane vesiculation are related to cellular transport and membrane components trafficking. Endocytosis, formation of caveolae and caveosomes, as well as Golgi membranes traffic have been linked to the existence and dynamics of particular types of lipid/protein membrane domains, enriched in sphingolipids and cholesterol, called rafts [Nature 387 (1997) 569; Trends Cell Biol. 12 (2002) 296; Biochemistry 27 (1988) 6197]. In addition, the participation of phospholipases in the vesiculation of Golgi and other membranes has been already established [Traffic 1 (2000) 504] essentially in their role in the production of second messenger molecules. In this work we illustrate with raft-containing giant lipid vesicles a mechanism for raft-vesicle expulsion from the membrane due to the activity of a single enzyme-phospholipase A(2) (PLA(2)). This leads to the hypothesis that the PLA(2), apart from its role in second messenger generation, might play a direct and general role in the vesiculation processes underlying the intermembrane transport of rafts through purely physicochemical mechanisms. These mechanisms would be: enzyme adsorption leading to membrane curvature generation (budding), and enzyme activity modulation of the line tension at the raft boundaries, which induces vesicle fission.