| http://purl.uniprot.org/citations/17895371 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17895371 | http://www.w3.org/2000/01/rdf-schema#comment | "Niemann-Pick Type C (NP-C) disease, caused by mutations in either human NPC1 (hNPC1) or human NPC2 (hNPC2), is characterized by the accumulation of unesterified cholesterol in late endosomes. Although it is known that the NP-C proteins are targeted to late endosomal/lysosomal compartments, their delivery mechanisms have not been fully elucidated. To identify mechanisms regulating NP-C protein localization, we used Saccharomyces cerevisiae, which expresses functional homologs of both NP-C proteins - scNcr1p and scNpc2p. Targeting of scNcr1p to the vacuole was perturbed in AP-3-deficient yeast cells, whereas the delivery of scNpc2p was affected by deficiencies in either AP-3 or GGA. We focused on the role of the AP-3 pathway in the targeting of the mammalian NP-C proteins. We found that, although mouse NPC1 (mNPC1) and hNPC2 co-localize with AP-3 to a similar extent in fibroblasts, hNPC2 preferentially co-localizes with AP-1. Importantly, the targeting of both mammalian NPC1 and NPC2 is dependent on AP-3. Moreover, and consistent with the NP-C proteins playing a role in cholesterol metabolism, AP-3-deficient cells have reduced levels of cholesterol. These results provide information about how the NP-C proteins are targeted to their sites of action and illustrate the possibility that defective sorting of the NP-C proteins along the endocytic route can alter cellular cholesterol."xsd:string |
| http://purl.uniprot.org/citations/17895371 | http://purl.org/dc/terms/identifier | "doi:10.1242/jcs.03487"xsd:string |
| http://purl.uniprot.org/citations/17895371 | http://purl.uniprot.org/core/author | "Werner E."xsd:string |
| http://purl.uniprot.org/citations/17895371 | http://purl.uniprot.org/core/author | "Faundez V."xsd:string |
| http://purl.uniprot.org/citations/17895371 | http://purl.uniprot.org/core/author | "Salazar G."xsd:string |
| http://purl.uniprot.org/citations/17895371 | http://purl.uniprot.org/core/author | "Styers M.L."xsd:string |
| http://purl.uniprot.org/citations/17895371 | http://purl.uniprot.org/core/author | "Maue R.A."xsd:string |
| http://purl.uniprot.org/citations/17895371 | http://purl.uniprot.org/core/author | "Berger A.C."xsd:string |
| http://purl.uniprot.org/citations/17895371 | http://purl.uniprot.org/core/author | "Corbett A.H."xsd:string |
| http://purl.uniprot.org/citations/17895371 | http://purl.uniprot.org/core/author | "Newell-Litwa K.A."xsd:string |
| http://purl.uniprot.org/citations/17895371 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17895371 | http://purl.uniprot.org/core/name | "J Cell Sci"xsd:string |
| http://purl.uniprot.org/citations/17895371 | http://purl.uniprot.org/core/pages | "3640-3652"xsd:string |
| http://purl.uniprot.org/citations/17895371 | http://purl.uniprot.org/core/title | "The subcellular localization of the Niemann-Pick Type C proteins depends on the adaptor complex AP-3."xsd:string |
| http://purl.uniprot.org/citations/17895371 | http://purl.uniprot.org/core/volume | "120"xsd:string |
| http://purl.uniprot.org/citations/17895371 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17895371 |
| http://purl.uniprot.org/citations/17895371 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17895371 |
| http://purl.uniprot.org/uniprot/P38153#attribution-4C2808BD492E8C45C651010364A3608E | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/17895371 |
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| http://purl.uniprot.org/uniprot/P46682#attribution-4C2808BD492E8C45C651010364A3608E | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/17895371 |
| http://purl.uniprot.org/uniprot/Q08951#attribution-4C2808BD492E8C45C651010364A3608E | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/17895371 |
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