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UNC-11, a Caenorhabditis elegans AP180 Homologue, Regulates the Size and Protein Composition of Synaptic Vesicles

Nonet, Michael L., Holgado, Andrea M., Brewer, Faraha, Serpe, Craig J., Norbeck, Betty A., Holleran, Julianne, Wei, Liping, Hartwieg, Erika, Jorgensen, Erik M., Alfonso, Aixa·1999·Molecular Biology of the Cell
DOI 10.1091/mbc.10.7.2343
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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-11mutants 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.

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Metadata

Authors
Nonet, M. L., Holgado, A. M., Brewer, F., Serpe, C. J., Norbeck, B. A., Holleran, J., Wei, L., Hartwieg, E., Jorgensen, E. M., & Alfonso, A.
Venue
Molecular Biology of the Cell
Publisher
American Society for Cell Biology (ASCB)
Published
1999-07
Volume
10
Issue
7
Pages
2343-2360
ISSN
  • 1059-1524
  • 1939-4586
DOI
10.1091/mbc.10.7.2343
Cited by
235
References
0
Language
en

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