RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/22822152http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22822152http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22822152http://www.w3.org/2000/01/rdf-schema#comment"Defective catabolite export from lysosomes results in lysosomal storage diseases in humans. Mutations in the cystine transporter gene CTNS cause cystinosis, but other lysosomal amino acid transporters are poorly characterized at the molecular level. Here, we identified the Caenorhabditis elegans lysosomal lysine/arginine transporter LAAT-1. Loss of laat-1 caused accumulation of lysine and arginine in enlarged, degradation-defective lysosomes. In mutants of ctns-1 (C. elegans homolog of CTNS), LAAT-1 was required to reduce lysosomal cystine levels and suppress lysosome enlargement by cysteamine, a drug that alleviates cystinosis by converting cystine to a lysine analog. LAAT-1 also maintained availability of cytosolic lysine/arginine during embryogenesis. Thus, LAAT-1 is the lysosomal lysine/arginine transporter, which suggests a molecular explanation for how cysteamine alleviates a lysosomal storage disease."xsd:string
http://purl.uniprot.org/citations/22822152http://purl.org/dc/terms/identifier"doi:10.1126/science.1220281"xsd:string
http://purl.uniprot.org/citations/22822152http://purl.org/dc/terms/identifier"doi:10.1126/science.1220281"xsd:string
http://purl.uniprot.org/citations/22822152http://purl.uniprot.org/core/author"Du H."xsd:string
http://purl.uniprot.org/citations/22822152http://purl.uniprot.org/core/author"Du H."xsd:string
http://purl.uniprot.org/citations/22822152http://purl.uniprot.org/core/author"Liu B."xsd:string
http://purl.uniprot.org/citations/22822152http://purl.uniprot.org/core/author"Liu B."xsd:string
http://purl.uniprot.org/citations/22822152http://purl.uniprot.org/core/author"Wang X."xsd:string
http://purl.uniprot.org/citations/22822152http://purl.uniprot.org/core/author"Wang X."xsd:string
http://purl.uniprot.org/citations/22822152http://purl.uniprot.org/core/author"Gartner A."xsd:string
http://purl.uniprot.org/citations/22822152http://purl.uniprot.org/core/author"Gartner A."xsd:string
http://purl.uniprot.org/citations/22822152http://purl.uniprot.org/core/author"Rutkowski R."xsd:string
http://purl.uniprot.org/citations/22822152http://purl.uniprot.org/core/author"Rutkowski R."xsd:string
http://purl.uniprot.org/citations/22822152http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22822152http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22822152http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/22822152http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/22822152http://purl.uniprot.org/core/pages"351-354"xsd:string
http://purl.uniprot.org/citations/22822152http://purl.uniprot.org/core/pages"351-354"xsd:string
http://purl.uniprot.org/citations/22822152http://purl.uniprot.org/core/title"LAAT-1 is the lysosomal lysine/arginine transporter that maintains amino acid homeostasis."xsd:string
http://purl.uniprot.org/citations/22822152http://purl.uniprot.org/core/title"LAAT-1 is the lysosomal lysine/arginine transporter that maintains amino acid homeostasis."xsd:string
http://purl.uniprot.org/citations/22822152http://purl.uniprot.org/core/volume"337"xsd:string
http://purl.uniprot.org/citations/22822152http://purl.uniprot.org/core/volume"337"xsd:string