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J Biol Chem, Vol. 274, Issue 27, 18893-18901, July 2, 1999
From the Center for Basic Neuroscience, Department of Molecular
Genetics and Howard Hughes Medical Institute, The University of
Texas Southwestern Medical Center, Dallas, Texas 75235-9050
Synaptogyrins constitute a family of synaptic
vesicle proteins of unknown function. With the full-length structure of
a new brain synaptogyrin isoform, we now show that the synaptogyrin family in vertebrates includes two neuronal and one ubiquitous isoform.
All of these synaptogyrins are composed of a short conserved N-terminal
cytoplasmic sequence, four homologous transmembrane regions, and a
variable cytoplasmic C-terminal tail that is tyrosine-phosphorylated. The localization, abundance, and conservation of synaptogyrins suggest
a function in exocytosis. To test this, we employed a secretion assay
in PC12 cells expressing transfected human growth hormone (hGH) as a
reporter protein. When Ca2+-dependent hGH
secretion from PC12 cells was triggered by high K+ or
-latrotoxin, co-transfection of all synaptogyrins with hGH inhibited
hGH exocytosis as strongly as co-transfection of tetanus toxin light
chain. Synaptophysin I, which is distantly related to synaptogyrins,
was also inhibitory but less active. Inhibition was independent of the
amount of hGH expressed but correlated with the amount of synaptogyrin
transfected. Inhibition of exocytosis was not observed with several
other synaptic proteins, suggesting specificity. Analysis of the
regions of synaptogyrin required for inhibition revealed that the
conserved N-terminal domain of synaptogyrin is essential for
inhibition, whereas the long C-terminal cytoplasmic tail is largely
dispensable. Our results suggest that synaptogyrins are conserved
components of the exocytotic apparatus, which function as regulators of
Ca2+-dependent exocytosis.
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