Defects in synaptic vesicle docking in unc-18 mutants

Robby M. Weimer, Janet E. Richmond, Warren S. Davis, Gayla Hadwiger, Michael L. Nonet, Erik M. Jorgensen

Research output: Contribution to journalArticlepeer-review

193 Scopus citations

Abstract

Sec1-related proteins function in most, if not all, membrane trafficking pathways in eukaryotic cells. The Sec1-related protein required in neurons for synaptic vesicle exocytosis is UNC-18. Several models for UNC-18 function during vesicle exocytosis are under consideration. We have tested these models by characterizing unc-18 mutants of the nematode Caenorhabditis elegans. In the absence of UNC-18, the size of the readily releasable pool is severely reduced. Our results show that the near absence of fusion-competent vesicles is not caused by a reduction in syntaxin levels, by a mislocalization of syntaxin, by a defect in fusion or by a failure to open syntaxin during priming. Rather, we found a reduction of docked vesicles at the active zone in unc-18 mutants, suggesting that UNC-18 functions, directly or indirectly, as a facilitator of vesicle docking.

Original languageEnglish
Pages (from-to)1023-1030
Number of pages8
JournalNature neuroscience
Volume6
Issue number10
DOIs
StatePublished - Oct 1 2003

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