Abstract
Septins are GTPases required for the completion of cytokinesis in diverse organisms, yet their roles in cytokinesis or other cellular processes remain unknown. Here we describe studies of a newly identified septin, CDCrel-1, which is predominantly expressed in the nervous system. This protein was associated with membrane fractions, and a significant fraction of the protein copurified and coprecipitated with synaptic vesicles. In detergent extracts, CDCrel-1 and another septin, Nedd5, immunoprecipitated with the SNARE protein syntaxin by directly binding to syntaxin via the SNARE interaction domain. Transfection of HIT-T15 cells with wild-type CDCrel-1 inhibited secretion, whereas GTPase dominant-negative mutants enhanced secretion. These data suggest that septins may regulate vesicle dynamics through interactions with syntaxin.
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Acknowledgements
The authors thank G. Boulianne for comments on the manuscript. This work was supported by grant MT-13465 from the Medical Research Council of Canada to WST and NIH grant AG13208 to RB.
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Beites, C., Xie, H., Bowser, R. et al. The septin CDCrel-1 binds syntaxin and inhibits exocytosis. Nat Neurosci 2, 434–439 (1999). https://doi.org/10.1038/8100
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DOI: https://doi.org/10.1038/8100
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