Abstract
Synexin is a calcium binding protein of 47,000da which causes chromaffin granules (1–5) and chromaffin granule ghosts (6), as well as acidic liposomes (7,8) to aggregate and fuse. In addition to binding to granule membranes and liposomes, synexin also binds selectively to the inner aspect of chromaffin cell plasma membranes (9). Furthermore, synexin dependent fusion structures of chromaffin granules appear quite similar to the large vacuolar, compound exocytotic structures seen in secreting chromaffin cells (3–5). These facts have lead us to anticipate that synexin might be involved in fusion processes occurring during exocytosis (5). We have therefore devoted substantial efforts to trying to understand how synexin indeed fuses these biological and artificial membranes.
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© 1988 Plenum Press, New York
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Pollard, H.B., Rojas, E., Burns, A.L., Parra, C. (1988). Synexin, Calcium and the Hydrophobic Bridge Hypothesis for Membrane Fusion. In: Ohki, S., Doyle, D., Flanagan, T.D., Hui, S.W., Mayhew, E. (eds) Molecular Mechanisms of Membrane Fusion. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1659-6_25
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DOI: https://doi.org/10.1007/978-1-4613-1659-6_25
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