| pubmed-article:18596236 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18596236 | lifeskim:mentions | umls-concept:C0288881 | lld:lifeskim |
| pubmed-article:18596236 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:18596236 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:18596236 | lifeskim:mentions | umls-concept:C0599896 | lld:lifeskim |
| pubmed-article:18596236 | lifeskim:mentions | umls-concept:C0589502 | lld:lifeskim |
| pubmed-article:18596236 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:18596236 | pubmed:dateCreated | 2008-8-29 | lld:pubmed |
| pubmed-article:18596236 | pubmed:abstractText | The SM protein UNC-18 has been proposed to regulate several aspects of secretion, including synaptic vesicle docking, priming, and fusion. Here, we show that UNC-18 has a chaperone function in neurons, promoting anterograde transport of the plasma membrane soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) protein Syntaxin-1. In unc-18 mutants, UNC-64 (Caenorhabditis elegans Syntaxin-1) accumulates in neuronal cell bodies. Colocalization studies and analysis of carbohydrate modifications both suggest that this accumulation occurs in the endoplasmic reticulum. This trafficking defect is specific for UNC-64 Syntaxin-1, because 14 other SNARE proteins and two active zone markers were unaffected. UNC-18 binds to Syntaxin through at least two mechanisms: binding to closed Syntaxin, or to the N terminus of Syntaxin. It is unclear which of these binding modes mediates UNC-18 function in neurons. The chaperone function of UNC-18 was eliminated in double mutants predicted to disrupt both modes of Syntaxin binding, but it was unaffected in single mutants. By contrast, mutations predicted to disrupt UNC-18 binding to the N terminus of Syntaxin caused significant defects in locomotion behavior and responsiveness to cholinesterase inhibitors. Collectively, these results demonstrate the UNC-18 acts as a molecular chaperone for Syntaxin transport in neurons and that the two modes of UNC-18 binding to Syntaxin are involved in different aspects of UNC-18 function. | lld:pubmed |
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| pubmed-article:18596236 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18596236 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18596236 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18596236 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18596236 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:18596236 | pubmed:issn | 1939-4586 | lld:pubmed |
| pubmed-article:18596236 | pubmed:author | pubmed-author:KaplanJoshua... | lld:pubmed |
| pubmed-article:18596236 | pubmed:author | pubmed-author:McEwenJason... | lld:pubmed |
| pubmed-article:18596236 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18596236 | pubmed:volume | 19 | lld:pubmed |
| pubmed-article:18596236 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18596236 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18596236 | pubmed:pagination | 3836-46 | lld:pubmed |
| pubmed-article:18596236 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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