UNC-11, a Caenorhabditis elegans AP180 homologue, regulates the size and protein composition of synaptic vesicles

Michael L. Nonet, Andrea M. Holgado, Faraha Brewer, Craig J. Serpe, Betty A. Norbeck, Julianne Holleran, Liping Wei, Erika Hartwieg, Erik M. Jorgensen, Aixa Alfonso

Research output: Contribution to journalArticlepeer-review

225 Scopus citations

Abstract

The unc-11 gene of Caenorhabditis elegans encodes multiple isoforms of a protein homologous to the mammalian brain-specific clathrin-adaptor protein AP180. The UNC-11 protein is expressed at high levels in the nervous system and at lower levels in other tissues. In neurons, UNC-11 is enriched at presynaptic terminals but is also present in cell bodies, unc-11 mutants are defective in two aspects of synaptic vesicle biogenesis. First, the SNARE protein synaptobrevin is mislocalized, no longer being exclusively localized to synaptic vesicles. The reduction of synaptobrevin at synaptic vesicles is the probable cause of the reduced neurotransmitter release observed in these mutants. Second, unc-11 mutants accumulate large vesicles at synapses. We propose that the UNC-11 protein mediates two functions during synaptic vesicle biogenesis: it recruits synaptobrevin to synaptic vesicle membranes and it regulates the size of the budded vesicle during clathrin coat assembly.

Original languageEnglish
Pages (from-to)2343-2360
Number of pages18
JournalMolecular biology of the cell
Volume10
Issue number7
DOIs
StatePublished - Jul 1999

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