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J Biol Chem, Vol. 274, Issue 32, 22871-22876, August 6, 1999
From the The molecular basis of exocytotic membrane fusion
in the pancreatic acinar cell was investigated using an in
vitro assay that measures both zymogen granule-plasma membrane
fusion and granule-granule fusion. These two fusion events were
differentially sensitive to Ca2+, suggesting that they are
controlled by different Ca2+-sensing mechanisms. Botulinum
neurotoxin C (BoNT/C) treatment of the plasma membranes caused cleavage
of syntaxin 2, the apical isoform of this Q-SNARE, but did not affect
syntaxin 4, the basolateral isoform. BoNT/C also cleaved syntaxin 3, the zymogen granule isoform. BoNT/C treatment of plasma membranes
abolished granule-plasma membrane fusion, whereas toxin treatment of
the granules reduced granule-plasma membrane fusion and abolished
granule-granule fusion. Tetanus toxin cleaved granule-associated
synaptobrevin 2 but caused only a small reduction in both
granule-plasma membrane fusion and granule-granule fusion. Our results
indicate that syntaxin 2 is the isoform that mediates fusion between
zymogen granules and the apical plasma membrane of the acinar cell.
Syntaxin 3 mediates granule-granule fusion, which might be involved in
compound exocytosis. In contrast, the major R-SNARE on the zymogen
granule remains to be identified.
Identification of SNAREs Involved in Regulated Exocytosis in the
Pancreatic Acinar Cell
,
Department of Pharmacology, University of
Cambridge, Cambridge, CB2 1QJ, United Kingdom and the
¶ Department of Neurobiology, Max Planck Institute for Biophysical
Chemistry, Am Fassberg, D-37077 Göttingen, Germany
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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