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J. Biol. Chem., Vol. 277, Issue 51, 50030-50035, December 20, 2002
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From the Department of Molecular & Cell Biology, University of
California, Berkeley, California 94720 and The soluble
N-ethylmaleimide-sensitive factor attachment protein of 25 kDa (SNAP-25) plays an important role in vesicle trafficking. Together with vesicle-associated membrane protein-2 (VAMP-2) and syntaxin, SNAP-25 forms a ternary complex implicated in docking and
fusion of secretory vesicles with the plasma membrane during exocytosis. These so-called SNARE proteins are believed to regulate tubulovesicle trafficking and fusion during the secretory cycle of the
gastric parietal cell. Here we examined the cellular localization and
functional importance of SNAP-25 in parietal cell cultures. Adenoviral
constructs were used to express SNAP-25 tagged with cyan fluorescent
protein, VAMP-2 tagged with yellow fluorescent protein, and
SNAP-25 in which the C-terminal 25 amino acids were deleted (SNAP-25
Localization and Function of Soluble
N-Ethylmaleimide-sensitive Factor Attachment Protein-25 and
Vesicle-associated Membrane Protein-2 in Functioning Gastric Parietal
Cells*
, and Department
of Pathology, University of Oklahoma, Health Sciences Center, Oklahoma
City, Oklahoma 73190
181-206). Membrane fractionation experiments and fluorescent
imaging showed that SNAP-25 is localized to the apical plasma membrane.
The expression of the mutant SNAP-25 181-226 inhibited the acid
secretory response of parietal cells. Also, SNAP 181-226 bound
poorly in vitro with recombinant syntaxin-1 compared with
wild type SNAP-25, indicating that pairing between syntaxin-1 and
SNAP-25 is required for parietal cell activation. Dual expression of
SNAP-25 tagged with cyan fluorescent protein and VAMP-2 tagged with
yellow fluorescent protein revealed a dynamic change in distribution
associated with acid secretion. In resting cells, SNAP-25 is at the
apical plasma membrane and VAMP-2 is associated with cytoplasmic
H,K-ATPase-rich tubulovesicles. After stimulation, the two proteins
co-localize on the apical plasma membrane. These data demonstrate the
functional significance of SNAP-25 as a SNARE protein in the parietal
cell and show the dynamic stimulation-associated redistribution of
VAMP-2 from H,K-ATPase-rich tubulovesicles to co-localize with SNAP-25
on the apical plasma membrane.
*
This work was supported in part by National Institutes of
Health Grants DK10141 and DK38972 (to J. G. F.), DK56292 (to X. Y.),
and NS35167 and NSF, National Institutes of Health Grant IBN0110980 (to
Y. L.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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