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Vol. 10, Issue 7, 2343-2360, July 1999
and
*Department of Anatomy and Neurobiology, Washington University
School of Medicine, St. Louis, Missouri 63110;
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.
Department of Biological Sciences, University of
Illinois at Chicago, Chicago, Illinois 60607; §Department
of Biology and Howard Hughes Medical Institute, Massachusetts Institute
of Technology, Cambridge, Massachusetts 02139; and
Department of Biology, University of Utah, Salt Lake
City, Utah 84112
Corresponding authors. E-mail addresses:
nonetm{at}thalamus.wustl.edu and aalfonso{at}uic.edu.
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