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http://purl.uniprot.org/citations/17260967http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17260967http://www.w3.org/2000/01/rdf-schema#comment"Leucine-rich repeat kinase 2 (LRRK2), a product of a causative gene for the autosomal-dominant form of familial Parkinson's disease (PARK8), harbors a Ras-like small GTP binding protein-like (ROC) domain besides the kinase domain, although the relationship between these two functional domains remains elusive. Here we show by thin-layer chromatographic analysis that LRRK2 stably binds GTP but lacks a GTPase activity in HEK293 and Neuro-2a cells. A ROC domain mutation that converts LRRK2 to a guanine nucleotide-free form (T1348N) abolishes the kinase activity of LRRK2 as well as its phosphate incorporation upon metabolic labeling. The phosphorylation of LRRK2 was inhibited by potential inhibitors for cyclic AMP-dependent protein kinase. These data suggest that binding of GTP to the ROC domain regulates the kinase activity of LRRK2 as well as its phosphorylation by other kinase(s)."xsd:string
http://purl.uniprot.org/citations/17260967http://purl.org/dc/terms/identifier"doi:10.1021/bi061960m"xsd:string
http://purl.uniprot.org/citations/17260967http://purl.uniprot.org/core/author"Takeda K."xsd:string
http://purl.uniprot.org/citations/17260967http://purl.uniprot.org/core/author"Iwatsubo T."xsd:string
http://purl.uniprot.org/citations/17260967http://purl.uniprot.org/core/author"Ichijo H."xsd:string
http://purl.uniprot.org/citations/17260967http://purl.uniprot.org/core/author"Katada T."xsd:string
http://purl.uniprot.org/citations/17260967http://purl.uniprot.org/core/author"Okai T."xsd:string
http://purl.uniprot.org/citations/17260967http://purl.uniprot.org/core/author"Ito G."xsd:string
http://purl.uniprot.org/citations/17260967http://purl.uniprot.org/core/author"Fujino G."xsd:string
http://purl.uniprot.org/citations/17260967http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17260967http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/17260967http://purl.uniprot.org/core/pages"1380-1388"xsd:string
http://purl.uniprot.org/citations/17260967http://purl.uniprot.org/core/title"GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease."xsd:string
http://purl.uniprot.org/citations/17260967http://purl.uniprot.org/core/volume"46"xsd:string
http://purl.uniprot.org/citations/17260967http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17260967
http://purl.uniprot.org/citations/17260967http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17260967
http://purl.uniprot.org/uniprot/Q5S007#attribution-2719E86199DE0FAAD308B16DFC57CE29http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/17260967
http://purl.uniprot.org/uniprot/#_A0A218N881-mappedCitation-17260967http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17260967
http://purl.uniprot.org/uniprot/#_A2VED2-mappedCitation-17260967http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17260967
http://purl.uniprot.org/uniprot/#_Q17RV3-mappedCitation-17260967http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17260967
http://purl.uniprot.org/uniprot/#_Q6MZN9-mappedCitation-17260967http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17260967
http://purl.uniprot.org/uniprot/#_Q5S007-mappedCitation-17260967http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17260967
http://purl.uniprot.org/uniprot/A0A218N881http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17260967
http://purl.uniprot.org/uniprot/Q5S007http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17260967