Sea urchin eggs provide an efficient in vitro model of exocytosis. We
have identified proteins in sea urchin eggs that cross-react with anti
bodies to mammalian synaptobrevin, synaptotagmin, SNAP-25, syntaxin an
d rab3a. We show that these proteins are localized to the sea urchin e
gg cortex, using western blotting and immunocytochemistry. Tetanus tox
in light chain cleaves the synaptobrevin-related protein in vitro and
inhibits calcium-induced exocytosis. These data demonstrate a conserva
tion between phyla of protein sequence and molecular mechanisms though
t to facilitate exocytosis and show that the sea urchin egg provides a
unique in vitro exocytotic model with which to study the conserved pr
otein machinery of membrane fusion during secretion.