中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
PolyQ-expanded huntingtin and ataxin-3 sequester ubiquitin adaptors hHR23B and UBQLN2 into aggregates via conjugated ubiquitin

文献类型:期刊论文

作者Yang, Hui1,2; Yue, Hong-Wei1; He, Wen-Tian1; Hong, Jun-Ye1; Jiang, Lei-Lei1; Hu, Hong-Yu1
刊名FASEB JOURNAL
出版日期2018
卷号32期号:6页码:2923-2933
ISSN号0892-6638
关键词Protein-quality Control Group-c Protein Polyglutamine Disease Alpha-synuclein Neurodegenerative Diseases Parkinsons-disease Nuclear Inclusions Nucleocytoplasmic Transport Deubiquitinating Function Cytoplasmic Inclusions
DOI10.1096/fj.201700801RR
文献子类Article
英文摘要

The components of ubiquitin (Ub)-proteasome system, such as Ub, Ub adaptors, or proteasome subunits, are commonly accumulated with the aggregated proteins in inclusions, but how protein aggregates sequester Ub-related proteins remains elusive. Using N-terminal huntingtin (Htt-N552) and ataxin (Atx)-3 as model proteins, we investigated the molecular mechanism underlying sequestration of Ub adaptors by polyQ-expanded proteins. We found that polyQ-expanded Htt-N552 and Atx-3 sequester endogenous Ub adaptors, human RAD23 homolog B (hHR23B) and ubiquilin (UBQLN)-2, into inclusions. This sequestration effect is dependent on the UBA domains of Ub adaptors and the conjugated Ub of the aggregated proteins. Moreover, polyQ-expanded Htt-N552 and Atx-3 reduce the protein level of xeroderma pigmentosum group C (XPC) by sequestration of hHR23B, suggesting that this process may cut down the available quantity of hHR23B and thus affect its normal function in stabilizing XPC. Our findings demonstrate that polyQ-expanded proteins sequester Ub adaptors or other Ub-related proteins into aggregates or inclusions through ubiquitination of the pathogenic proteins. This study may also provide a common mechanism for the formation of Ub-positive inclusions in cells.-Yang, H., Yue, H.-W., He, W.-T., Hong, J.-Y., Jiang, L.-L., Hu, H.-Y. PolyQ-expanded huntingtin and ataxin-3 sequester ubiquitin adaptors hHR23B and UBQLN2 into aggregates via conjugated ubiquitin.

电子版国际标准刊号1530-6860
WOS研究方向Biochemistry & Molecular Biology ; Biology ; Cell Biology
语种英语
WOS记录号WOS:000432546000004
版本出版稿
源URL[http://202.127.25.143/handle/331003/3452]  
专题生化所2018年发文
上海生化细胞研究所_上海生科院生化细胞研究所
通讯作者Hu, Hong-Yu
作者单位1.Univ CAS, State Key Lab Mol Biol, CAS, Ctr Excellence Mol Cell Sci,SIBCB, Shanghai, Peoples R China;
2.Fudan Univ, Collaborat Innovat Ctr Genet & Dev, Sch Life Sci, State Key Lab Genet Engn, Shanghai, Peoples R China
推荐引用方式
GB/T 7714
Yang, Hui,Yue, Hong-Wei,He, Wen-Tian,et al. PolyQ-expanded huntingtin and ataxin-3 sequester ubiquitin adaptors hHR23B and UBQLN2 into aggregates via conjugated ubiquitin[J]. FASEB JOURNAL,2018,32(6):2923-2933.
APA Yang, Hui,Yue, Hong-Wei,He, Wen-Tian,Hong, Jun-Ye,Jiang, Lei-Lei,&Hu, Hong-Yu.(2018).PolyQ-expanded huntingtin and ataxin-3 sequester ubiquitin adaptors hHR23B and UBQLN2 into aggregates via conjugated ubiquitin.FASEB JOURNAL,32(6),2923-2933.
MLA Yang, Hui,et al."PolyQ-expanded huntingtin and ataxin-3 sequester ubiquitin adaptors hHR23B and UBQLN2 into aggregates via conjugated ubiquitin".FASEB JOURNAL 32.6(2018):2923-2933.

入库方式: OAI收割

来源:上海生物化学与细胞生物学研究所

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