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http://purl.uniprot.org/citations/18675823http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18675823http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18675823http://www.w3.org/2000/01/rdf-schema#comment"Hypertonia, which is characterized by stiff gait, abnormal posture, jerky movements, and tremor, is associated with a number of neurological disorders, including cerebral palsy, dystonia, Parkinson's disease, stroke, and spinal cord injury. Recently, a spontaneous mutation in the gene encoding trafficking protein, kinesin-binding 1 (Trak1), was identified as the genetic defect that causes hypertonia in mice. The subcellular localization and biological function of Trak1 remain unclear. Here we report that Trak1 interacts with hepatocyte-growth-factor-regulated tyrosine kinase substrate (Hrs), an essential component of the endosomal sorting and trafficking machinery. Double-label immunofluorescence confocal studies show that the endogenous Trak1 protein partially colocalizes with Hrs on early endosomes. Like Hrs, both overexpression and small-interfering-RNA-mediated knockdown of Trak1 inhibit degradation of internalized epidermal growth factor receptors through a block in endosome-to-lysosome trafficking. Our findings support a role for Trak1 in the regulation of Hrs-mediated endosomal sorting and have important implications for understanding hypertonia associated with neurological disorders."xsd:string
http://purl.uniprot.org/citations/18675823http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2008.07.045"xsd:string
http://purl.uniprot.org/citations/18675823http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2008.07.045"xsd:string
http://purl.uniprot.org/citations/18675823http://purl.uniprot.org/core/author"Li L."xsd:string
http://purl.uniprot.org/citations/18675823http://purl.uniprot.org/core/author"Li L."xsd:string
http://purl.uniprot.org/citations/18675823http://purl.uniprot.org/core/author"Chin L.S."xsd:string
http://purl.uniprot.org/citations/18675823http://purl.uniprot.org/core/author"Chin L.S."xsd:string
http://purl.uniprot.org/citations/18675823http://purl.uniprot.org/core/author"Webber E."xsd:string
http://purl.uniprot.org/citations/18675823http://purl.uniprot.org/core/author"Webber E."xsd:string
http://purl.uniprot.org/citations/18675823http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18675823http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18675823http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/18675823http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/18675823http://purl.uniprot.org/core/pages"638-651"xsd:string
http://purl.uniprot.org/citations/18675823http://purl.uniprot.org/core/pages"638-651"xsd:string
http://purl.uniprot.org/citations/18675823http://purl.uniprot.org/core/title"Hypertonia-associated protein Trak1 is a novel regulator of endosome-to-lysosome trafficking."xsd:string
http://purl.uniprot.org/citations/18675823http://purl.uniprot.org/core/title"Hypertonia-associated protein Trak1 is a novel regulator of endosome-to-lysosome trafficking."xsd:string
http://purl.uniprot.org/citations/18675823http://purl.uniprot.org/core/volume"382"xsd:string
http://purl.uniprot.org/citations/18675823http://purl.uniprot.org/core/volume"382"xsd:string
http://purl.uniprot.org/citations/18675823http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18675823
http://purl.uniprot.org/citations/18675823http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18675823
http://purl.uniprot.org/citations/18675823http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18675823
http://purl.uniprot.org/citations/18675823http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18675823