論文 - 詳細
| 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 |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 最多言及媒体 | X(Twitter) |
| 各媒体での言及数の合計 | 4 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| 線虫 | tm2899 |