RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/24687852http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24687852http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24687852http://www.w3.org/2000/01/rdf-schema#comment"Mutations in the leucine-rich repeat kinase 2 gene (LRRK2) are associated with familial and sporadic Parkinson's disease (PD). LRRK2 is a complex protein that consists of multiple domains, including predicted C-terminal WD40 repeats. In this study, we analyzed functional and molecular features conferred by the WD40 domain. Electron microscopic analysis of the purified LRRK2 C-terminal domain revealed doughnut-shaped particles, providing experimental evidence for its WD40 fold. We demonstrate that LRRK2 WD40 binds and sequesters synaptic vesicles via interaction with vesicle-associated proteins. In fact, a domain-based pulldown approach combined with mass spectrometric analysis identified LRRK2 as being part of a highly specific protein network involved in synaptic vesicle trafficking. In addition, we found that a C-terminal sequence variant associated with an increased risk of developing PD, G2385R, correlates with a reduced binding affinity of LRRK2 WD40 to synaptic vesicles. Our data demonstrate a critical role of the WD40 domain within LRRK2 function."xsd:string
http://purl.uniprot.org/citations/24687852http://purl.org/dc/terms/identifier"doi:10.1128/mcb.00914-13"xsd:string
http://purl.uniprot.org/citations/24687852http://purl.org/dc/terms/identifier"doi:10.1128/mcb.00914-13"xsd:string
http://purl.uniprot.org/citations/24687852http://purl.uniprot.org/core/author"Jagtap P."xsd:string
http://purl.uniprot.org/citations/24687852http://purl.uniprot.org/core/author"Jagtap P."xsd:string
http://purl.uniprot.org/citations/24687852http://purl.uniprot.org/core/author"Pan L."xsd:string
http://purl.uniprot.org/citations/24687852http://purl.uniprot.org/core/author"Pan L."xsd:string
http://purl.uniprot.org/citations/24687852http://purl.uniprot.org/core/author"Sattler M."xsd:string
http://purl.uniprot.org/citations/24687852http://purl.uniprot.org/core/author"Sattler M."xsd:string
http://purl.uniprot.org/citations/24687852http://purl.uniprot.org/core/author"Weinkauf S."xsd:string
http://purl.uniprot.org/citations/24687852http://purl.uniprot.org/core/author"Weinkauf S."xsd:string
http://purl.uniprot.org/citations/24687852http://purl.uniprot.org/core/author"Zhang M."xsd:string
http://purl.uniprot.org/citations/24687852http://purl.uniprot.org/core/author"Zhang M."xsd:string
http://purl.uniprot.org/citations/24687852http://purl.uniprot.org/core/author"Sala C."xsd:string
http://purl.uniprot.org/citations/24687852http://purl.uniprot.org/core/author"Sala C."xsd:string
http://purl.uniprot.org/citations/24687852http://purl.uniprot.org/core/author"Gloeckner C.J."xsd:string
http://purl.uniprot.org/citations/24687852http://purl.uniprot.org/core/author"Gloeckner C.J."xsd:string
http://purl.uniprot.org/citations/24687852http://purl.uniprot.org/core/author"Marte A."xsd:string
http://purl.uniprot.org/citations/24687852http://purl.uniprot.org/core/author"Marte A."xsd:string
http://purl.uniprot.org/citations/24687852http://purl.uniprot.org/core/author"Ueffing M."xsd:string
http://purl.uniprot.org/citations/24687852http://purl.uniprot.org/core/author"Ueffing M."xsd:string
http://purl.uniprot.org/citations/24687852http://purl.uniprot.org/core/author"Vogt A."xsd:string
http://purl.uniprot.org/citations/24687852http://purl.uniprot.org/core/author"Vogt A."xsd:string