| pubmed-article:18006691 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18006691 | lifeskim:mentions | umls-concept:C0596981 | lld:lifeskim |
| pubmed-article:18006691 | lifeskim:mentions | umls-concept:C0521390 | lld:lifeskim |
| pubmed-article:18006691 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:18006691 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:18006691 | lifeskim:mentions | umls-concept:C0019868 | lld:lifeskim |
| pubmed-article:18006691 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:18006691 | lifeskim:mentions | umls-concept:C0162610 | lld:lifeskim |
| pubmed-article:18006691 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:18006691 | pubmed:dateCreated | 2007-11-16 | lld:pubmed |
| pubmed-article:18006691 | pubmed:abstractText | Protein homeostasis maintains proper intracellular balance by promoting protein folding and clearance mechanisms while minimizing the stress caused by the accumulation of misfolded and damaged proteins. Chronic expression of aggregation-prone proteins is deleterious to the cell and has been linked to a wide range of conformational disorders. The molecular response to misfolded proteins is highly conserved and generally studied as a cell-autonomous process. Here, we provide evidence that neuronal signaling is an important modulator of protein homeostasis in post-synaptic muscle cells. In a forward genetic screen in Caenorhabditis elegans for enhancers of polyglutamine aggregation in muscle cells, we identified unc-30, a neuron-specific transcription factor that regulates the synthesis of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA). We used additional sensors of protein conformational states to show that defective GABA signaling or increased acetylcholine (ACh) signaling causes a general imbalance in protein homeostasis in post-synaptic muscle cells. Moreover, exposure to GABA antagonists or ACh agonists has a similar effect, which reveals that toxins that act at the neuromuscular junction are potent modifiers of protein conformational disorders. These results demonstrate the importance of intercellular communication in intracellular homeostasis. | lld:pubmed |
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| pubmed-article:18006691 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18006691 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18006691 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18006691 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18006691 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18006691 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:18006691 | pubmed:issn | 0890-9369 | lld:pubmed |
| pubmed-article:18006691 | pubmed:author | pubmed-author:MorimotoRicha... | lld:pubmed |
| pubmed-article:18006691 | pubmed:author | pubmed-author:AmaralMargari... | lld:pubmed |
| pubmed-article:18006691 | pubmed:author | pubmed-author:GarciaSusana... | lld:pubmed |
| pubmed-article:18006691 | pubmed:author | pubmed-author:CasanuevaM... | lld:pubmed |
| pubmed-article:18006691 | pubmed:author | pubmed-author:SilvaM... | lld:pubmed |
| pubmed-article:18006691 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18006691 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:18006691 | pubmed:volume | 21 | lld:pubmed |
| pubmed-article:18006691 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18006691 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18006691 | pubmed:pagination | 3006-16 | lld:pubmed |
| pubmed-article:18006691 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:18006691 | pubmed:meshHeading | pubmed-meshheading:18006691... | lld:pubmed |
