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 |
DOI | 10.1096/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. |
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