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J Biol Chem, Vol. 273, Issue 35, 22217-22223, August 28, 1998

Synaptotagmin-1 Is Required for Fibroblast Growth Factor-1 Release

Theresa M. LaVallee, Francesca Tarantini§, Susan Gamble, Carla Mouta Carreira§, Anthony Jackson, and Thomas Maciag§

From the Department of Molecular Biology, Holland Laboratory, American Red Cross, Rockville, Maryland 20855 and the § Center for Molecular Medicine, Maine Medical Center Research Institute, South Portland, Maine 04106

By using p65 synaptotagmin-1 and fibroblast growth factor (FGF)-1:beta -galactosidase (beta -gal) NIH 3T3 cell co-transfectants, we demonstrate that a proteolytic fragment consisting of the extravesicular domain of synaptotagmin-1 is released into the extracellular compartment in response to temperature stress with similar kinetics and pharmacological properties as FGF-1:beta -gal. Using a deletion mutant that lacks 95 amino acids from the extravesicular domain of synaptotagmin-1, neither synaptotagmin-1 nor FGF-1:beta -gal are able to access the stress-induced release pathway. Furthermore, the p40 extravesicular fragment of synaptotagmin-1 is constitutively released in p40 synaptotagmin-1 NIH 3T3 cell transfectants, and this release is potentiated when the cells are subjected to temperature stress. These data demonstrate that the p40 fragment derived from synaptotagmin-1 is able to utilize the FGF-1 non-classical exocytotic pathway and that the release of FGF-1 is dependent on synaptotagmin-1.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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