RRC ID 37021
著者 Fukuzono T, Pastuhov SI, Fukushima O, Li C, Hattori A, Iemura S, Natsume T, Shibuya H, Hanafusa H, Matsumoto K, Hisamoto N.
タイトル Chaperone complex BAG2-HSC70 regulates localization of Caenorhabditis elegans leucine-rich repeat kinase LRK-1 to the Golgi.
ジャーナル Genes Cells
Abstract Mutations in LRRK2 are linked to autosomal dominant forms of Parkinson's disease. We identified two human proteins that bind to LRRK2: BAG2 and HSC70, which are known to form a chaperone complex. We characterized the role of their Caenorhabditis elegans homologues, UNC-23 and HSP-1, in the regulation of LRK-1, the sole homologue of human LRRK2. In C. elegans, LRK-1 determines the polarized sorting of synaptic vesicle (SV) proteins to the axons by excluding SV proteins from the dendrite-specific transport machinery in the Golgi. In unc-23 mutants, SV proteins are localized to both presynaptic and dendritic endings in neurons, a phenotype also observed in lrk-1 deletion mutants. Furthermore, we isolated mutations in the hsp-1 gene that can suppress the unc-23, but not the lrk-1 defect. We show that UNC-23 determines LRK-1 localization to the Golgi apparatus in cooperation with HSP-1. These results describe a chaperone-dependent mechanism through which LRK-1 localization is regulated.
巻・号 21(4)
ページ 311-24
公開日 2016-4-1
DOI 10.1111/gtc.12338
PMID 26853528
MeSH Animals Caenorhabditis elegans / cytology Caenorhabditis elegans / metabolism* Caenorhabditis elegans Proteins / metabolism* Carrier Proteins / metabolism* Golgi Apparatus / metabolism* HSP70 Heat-Shock Proteins / metabolism* Molecular Chaperones / metabolism Protein Serine-Threonine Kinases / metabolism* Synaptic Vesicles / metabolism
IF 1.655
引用数 5
WOS 分野 GENETICS & HEREDITY CELL BIOLOGY
リソース情報
線虫 tm2899