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Vol. 9, Issue 6, 1235-1252, June 1998
Department of Anatomy and Neurobiology, Washington University
School of Medicine, St. Louis, Missouri 63110
We describe the molecular cloning and characterization of the
unc-64 locus of Caenorhabditis elegans.
unc-64 expresses three transcripts, each encoding a molecule
with 63-64% identity to human syntaxin 1A, a membrane- anchored
protein involved in synaptic vesicle fusion. Interestingly, the
alternative forms of syntaxin differ only in their C-terminal
hydrophobic membrane anchors. The forms are differentially expressed in
neuronal and secretory tissues; genetic evidence suggests that these
forms are not functionally equivalent. A complete loss-of-function
mutation in unc-64 results in a worm that completes
embryogenesis, but arrests development shortly thereafter as a
paralyzed L1 larva, presumably as a consequence of neuronal
dysfunction. The severity of the neuronal phenotypes of C.
elegans syntaxin mutants appears comparable to those of Drosophila syntaxin mutants. However, nematode syntaxin
appears not to be required for embryonic development, for secretion of cuticle from the hypodermis, or for the function of muscle, in contrast
to Drosophila syntaxin, which appears to be required in
all cells. Less severe viable unc-64 mutants exhibit a
variety of behavioral defects and show strong resistance to the
acetylcholinesterase inhibitor aldicarb. Extracellular physiological
recordings from pharyngeal muscle of hypomorphic mutants show
alterations in the kinetics of transmitter release. The lesions in the
hypomorphic alleles map to the hydrophobic face of the H3 coiled-coil
domain of syntaxin, a domain that in vitro mediates physical
interactions with similar coiled-coil domains in SNAP-25 and
synaptobrevin. Furthermore, the unc-64 syntaxin mutants
exhibit allele-specific genetic interactions with mutants carrying
lesions in the coiled-coil domain of synaptobrevin, providing in vivo
evidence for the significance of these domains in regulating synaptic
vesicle fusion.
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