Modulation of membrane fusion by calcium-binding proteins.
The effects of several Ca2+-binding proteins (calmodulin, prothrombin, and synexin) on the kinetics of Ca2+-induced membrane fusion were examined. Membrane fusion was assayed by following the mixing of aqueous contents of phospholipid vesicles. Calmodulin inhibited slightly the fusion of phospholipid vesicles. Bovine prothrombin and its proteolytic fragment 1 had a strong inhibitory effect on fusion. Depending on the phospholipid composition, synexin could either facilitate or inhibit Ca2+-induced fusion of vesicles. The effects of synexin were Ca2+ specific. 10 microM Ca2+ was sufficient to induce fusion of vesicles composed of phosphatidic acid/phosphatidylethanolamine (1:3) in the presence of synexin and 1 mM Mg2+. We propose that synexin may be involved in intracellular membrane fusion events mediated by Ca2+, such as exocytosis, and discuss possible mechanisms facilitating fusion.
D000818:Animals; D017310:Annexin A7; D002135:Calcium-Binding Proteins / Q000502:physiology*; D002147:Calmodulin / Q000494:pharmacology; D002417:Cattle; D004531:Eggs; D005089:Exocytosis / Q000187:drug effects; D066298:In Vitro Techniques; D007700:Kinetics; D008561:Membrane Fusion / Q000187:drug effects*; D008567:Membranes, Artificial; D008823:Micelles; D008954:Models, Biological; D010743:Phospholipids; D011506:Proteins / Q000494:pharmacology; D011516:Prothrombin / Q000494:pharmacology
D017310:Annexin A7; D002135:Calcium-Binding Proteins; D002147:Calmodulin; D008567:Membranes, Artificial; D008823:Micelles; D010743:Phospholipids; D011506:Proteins; D011516:Prothrombin