| http://purl.uniprot.org/citations/21983566 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21983566 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21983566 | http://www.w3.org/2000/01/rdf-schema#comment | "Cellular toxicity introduced by protein misfolding threatens cell fitness and viability. Failure to eliminate these polypeptides is associated with numerous aggregation diseases. Several protein quality control mechanisms degrade non-native proteins by the ubiquitin-proteasome system. Here, we use quantitative mass spectrometry to demonstrate that heat-shock triggers a large increase in the level of ubiquitylation associated with misfolding of cytosolic proteins. We discover that the Hul5 HECT ubiquitin ligase participates in this heat-shock stress response. Hul5 is required to maintain cell fitness after heat-shock and to degrade short-lived misfolded proteins. In addition, localization of Hul5 in the cytoplasm is important for its quality control function. We identify potential Hul5 substrates in heat-shock and physiological conditions to reveal that Hul5 is required for ubiquitylation of low-solubility cytosolic proteins including the Pin3 prion-like protein. These findings indicate that Hul5 is involved in a cytosolic protein quality control pathway that targets misfolded proteins for degradation."xsd:string |
| http://purl.uniprot.org/citations/21983566 | http://purl.org/dc/terms/identifier | "doi:10.1038/ncb2343"xsd:string |
| http://purl.uniprot.org/citations/21983566 | http://purl.org/dc/terms/identifier | "doi:10.1038/ncb2343"xsd:string |
| http://purl.uniprot.org/citations/21983566 | http://purl.uniprot.org/core/author | "Mayor T."xsd:string |
| http://purl.uniprot.org/citations/21983566 | http://purl.uniprot.org/core/author | "Mayor T."xsd:string |
| http://purl.uniprot.org/citations/21983566 | http://purl.uniprot.org/core/author | "Measday V."xsd:string |
| http://purl.uniprot.org/citations/21983566 | http://purl.uniprot.org/core/author | "Measday V."xsd:string |
| http://purl.uniprot.org/citations/21983566 | http://purl.uniprot.org/core/author | "Fang N.N."xsd:string |
| http://purl.uniprot.org/citations/21983566 | http://purl.uniprot.org/core/author | "Fang N.N."xsd:string |
| http://purl.uniprot.org/citations/21983566 | http://purl.uniprot.org/core/author | "Ng A.H."xsd:string |
| http://purl.uniprot.org/citations/21983566 | http://purl.uniprot.org/core/author | "Ng A.H."xsd:string |
| http://purl.uniprot.org/citations/21983566 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21983566 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21983566 | http://purl.uniprot.org/core/name | "Nat. Cell Biol."xsd:string |
| http://purl.uniprot.org/citations/21983566 | http://purl.uniprot.org/core/name | "Nat. Cell Biol."xsd:string |
| http://purl.uniprot.org/citations/21983566 | http://purl.uniprot.org/core/pages | "1344-1352"xsd:string |
| http://purl.uniprot.org/citations/21983566 | http://purl.uniprot.org/core/pages | "1344-1352"xsd:string |
| http://purl.uniprot.org/citations/21983566 | http://purl.uniprot.org/core/title | "Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins."xsd:string |
| http://purl.uniprot.org/citations/21983566 | http://purl.uniprot.org/core/title | "Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins."xsd:string |
| http://purl.uniprot.org/citations/21983566 | http://purl.uniprot.org/core/volume | "13"xsd:string |
| http://purl.uniprot.org/citations/21983566 | http://purl.uniprot.org/core/volume | "13"xsd:string |
| http://purl.uniprot.org/citations/21983566 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21983566 |
| http://purl.uniprot.org/citations/21983566 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21983566 |