Modulation of Membrane Fusion by Calcium-binding Proteins

Overview

Journal Biophys J

Publisher Cell Press

Specialty Biophysics

Date 1982 Jan 1

PMID 6459804

Citations 10

Authors

K Hong

N Duzgunes

D Papahadjopoulos

Affiliations

Soon will be listed here.

Abstract

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.

Citing Articles

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Synexin facilitates fusion of specific phospholipid membranes at divalent cation concentrations found intracellularly.

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