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Journal of Cell Science, Vol 110, Issue 14 1555-1561, Copyright © 1997 by Company of Biologists
JOURNAL ARTICLES |
J Avery, A Hodel and M Whitaker
Department of Physiological Sciences, Medical School, University of Newcastle upon Tyne, UK.
Sea urchin eggs provide an efficient in vitro model of exocytosis. We have identified proteins in sea urchin eggs that cross-react with antibodies to mammalian synaptobrevin, synaptotagmin, SNAP-25, syntaxin and rab3a. We show that these proteins are localized to the sea urchin egg cortex, using western blotting and immunocytochemistry. Tetanus toxin light chain cleaves the synaptobrevin-related protein in vitro and inhibits calcium-induced exocytosis. These data demonstrate a conservation between phyla of protein sequence and molecular mechanisms thought to facilitate exocytosis and show that the sea urchin egg provides a unique in vitro exocytotic model with which to study the conserved protein machinery of membrane fusion during secretion.
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