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http://purl.uniprot.org/citations/20173330http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20173330http://www.w3.org/2000/01/rdf-schema#comment"Increasing evidence supports a putative link between LRRK2 function and the MAP kinase cascades. We recently demonstrated that LRRK2 binds to MKK6, -3, and -7. Previous studies demonstrated that scaffold proteins are essential in the regulation of subcellular localization of stress kinase complexes. The c-jun NH2-terminal kinase (JNK)-interacting proteins (JIPs) are a group of scaffold proteins that play an important role in the regulation of MAP kinase signaling cascades. JIP1-3 are known to regulate the specificity and localization of the JNK pathway, while JIP4 is a specific scaffolding protein for the p38 pathway. We demonstrate that LRRK2 binds to JIP1-4, and is associated with increased levels of total JIP1, -3, -4, oligomeric JIP and ubiquitinated JIP. These results are consistent with a putative role of LRRK2 in regulating the stress kinase cascade."xsd:string
http://purl.uniprot.org/citations/20173330http://purl.org/dc/terms/identifier"doi:10.1159/000285509"xsd:string
http://purl.uniprot.org/citations/20173330http://purl.uniprot.org/core/author"Hsu C.H."xsd:string
http://purl.uniprot.org/citations/20173330http://purl.uniprot.org/core/author"Chan D."xsd:string
http://purl.uniprot.org/citations/20173330http://purl.uniprot.org/core/author"Wolozin B."xsd:string
http://purl.uniprot.org/citations/20173330http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20173330http://purl.uniprot.org/core/name"Neurodegener Dis"xsd:string
http://purl.uniprot.org/citations/20173330http://purl.uniprot.org/core/pages"68-75"xsd:string
http://purl.uniprot.org/citations/20173330http://purl.uniprot.org/core/title"LRRK2 and the stress response: interaction with MKKs and JNK-interacting proteins."xsd:string
http://purl.uniprot.org/citations/20173330http://purl.uniprot.org/core/volume"7"xsd:string
http://purl.uniprot.org/citations/20173330http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20173330
http://purl.uniprot.org/citations/20173330http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20173330
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http://purl.uniprot.org/uniprot/#_B8X349-mappedCitation-20173330http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20173330
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http://purl.uniprot.org/uniprot/#_F6WNT4-mappedCitation-20173330http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20173330
http://purl.uniprot.org/uniprot/#_F8WH31-mappedCitation-20173330http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20173330
http://purl.uniprot.org/uniprot/#_J3QNR6-mappedCitation-20173330http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20173330
http://purl.uniprot.org/uniprot/#_K3W4S4-mappedCitation-20173330http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20173330