| http://purl.uniprot.org/citations/23733886 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23733886 | http://www.w3.org/2000/01/rdf-schema#comment | "Low density lipoprotein (LDL) cholesterol is taken up into cells via clathrin-mediated endocytosis of the LDL receptor (LDLR). Following dissociation of the LDLR-LDL complex, LDL is directed to lysosomes whereas the LDLR recycles to the plasma membrane. Activation of the sterol-sensing nuclear receptors liver X receptors (LXRs) enhances degradation of the LDLR. This depends on the LXR target gene inducible degrader of the LDLR (IDOL), an E3-ubiquitin ligase that promotes ubiquitylation and lysosomal degradation of the LDLR. How ubiquitylation of the LDLR by IDOL controls its endocytic trafficking is currently unknown. Using genetic- and pharmacological-based approaches coupled to functional assessment of LDL uptake, we show that the LXR-IDOL axis targets a LDLR pool present in lipid rafts. IDOL-dependent internalization of the LDLR is independent of clathrin, caveolin, macroautophagy, and dynamin. Rather, it depends on the endocytic protein epsin. Consistent with LDLR ubiquitylation acting as a sorting signal, degradation of the receptor can be blocked by perturbing the endosomal sorting complex required for transport (ESCRT) or by USP8, a deubiquitylase implicated in sorting ubiquitylated cargo to multivesicular bodies. In summary, we provide evidence for the existence of an LXR-IDOL-mediated internalization pathway for the LDLR that is distinct from that used for lipoprotein uptake."xsd:string |
| http://purl.uniprot.org/citations/23733886 | http://purl.org/dc/terms/identifier | "doi:10.1194/jlr.m037713"xsd:string |
| http://purl.uniprot.org/citations/23733886 | http://purl.uniprot.org/core/author | "Sorrentino V."xsd:string |
| http://purl.uniprot.org/citations/23733886 | http://purl.uniprot.org/core/author | "Polo S."xsd:string |
| http://purl.uniprot.org/citations/23733886 | http://purl.uniprot.org/core/author | "Marques A.R.A."xsd:string |
| http://purl.uniprot.org/citations/23733886 | http://purl.uniprot.org/core/author | "Zelcer N."xsd:string |
| http://purl.uniprot.org/citations/23733886 | http://purl.uniprot.org/core/author | "Maspero E."xsd:string |
| http://purl.uniprot.org/citations/23733886 | http://purl.uniprot.org/core/author | "Scheer L."xsd:string |
| http://purl.uniprot.org/citations/23733886 | http://purl.uniprot.org/core/author | "Nelson J.K."xsd:string |
| http://purl.uniprot.org/citations/23733886 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23733886 | http://purl.uniprot.org/core/name | "J Lipid Res"xsd:string |
| http://purl.uniprot.org/citations/23733886 | http://purl.uniprot.org/core/pages | "2174-2184"xsd:string |
| http://purl.uniprot.org/citations/23733886 | http://purl.uniprot.org/core/title | "The LXR-IDOL axis defines a clathrin-, caveolae-, and dynamin-independent endocytic route for LDLR internalization and lysosomal degradation."xsd:string |
| http://purl.uniprot.org/citations/23733886 | http://purl.uniprot.org/core/volume | "54"xsd:string |
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