Aggregation of the 35-kDa fragment of TDP-43 causes formation of cytoplasmic inclusions and alteration of RNA processing
文献类型：期刊论文
| 作者 | Che, MX; Jiang, YJ; Xie, YY; Jiang, LL; Hu, HY |
| 刊名 | FASEB JOURNAL
 |
| 出版日期 | 2011 |
| 卷号 | 25期号:7页码:2344-2353 |
| 关键词 | delocalization amyotrophic lateral sclerosis TDP-35 seeding pre-mRNA splicing |
| 通讯作者 | Hu, HY (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, State Key Lab Mol Biol, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.,hyhu@sibs.ac.cn |
| 英文摘要 | TAR DNA binding protein of 43 kDa (TDP-43) is a nuclear factor functioning in RNA processing. It is also a major deposited protein in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration with ubiquitin (FTLD-U). To understand the mechanism underlying the inclusion body formation and possible functional alteration, we studied some TDP-43 fragments and their effects on RNA processing in cell models. The results show that the 35-kDa fragment of TDP-43 (namely TDP-35, residues 90-414), but not TDP-25A (184-414), is capable of forming cytoplasmic inclusion bodies and altering pre-mRNA splicing. The inclusions formed by TDP-35 can also recruit full-length TDP-43 to cytoplasmic deposition from functionally nuclear localization. The in vitro studies demonstrate that TDP-35, rather than TDP-43 and TDP-25A, is prone to aggregation, and it further serves as a seed to facilitate aggregation of full-length TDP-43. This suggests that fragmentation of TDP-43 leads to cellular redistribution, inclusion body formation, and altered RNA processing, which are implicated in the molecular pathogenesis of ALS and FTLD.-Che, M.-X., Jiang, Y.-J., Xie, Y.-Y., Jiang, L.-L., Hu, H.-Y. Aggregation of the 35-kDa fragment of TDP-43 causes formation of cytoplasmic inclusions and alteration of RNA processing. FASEB J. 25, 2344-2353 (2011). www.fasebj.org |
| 学科主题 | Biochemistry & Molecular Biology; Life Sciences & Biomedicine - Other Topics; Cell Biology |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biology ; Cell Biology |
| 关键词[WOS] | AMYOTROPHIC-LATERAL-SCLEROSIS ; FRONTOTEMPORAL LOBAR DEGENERATION ; DNA-BINDING PROTEIN-43 ; NUCLEAR FACTOR TDP-43 ; ALZHEIMERS-DISEASE ; NEURODEGENERATIVE DISEASES ; MESSENGER-RNA ; CFTR EXON-9 ; IN-VIVO ; MUTATIONS |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000292242200026 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/833]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Che, MX,Jiang, YJ,Xie, YY,et al. Aggregation of the 35-kDa fragment of TDP-43 causes formation of cytoplasmic inclusions and alteration of RNA processing[J]. FASEB JOURNAL,2011,25(7):2344-2353. |
| APA | Che, MX,Jiang, YJ,Xie, YY,Jiang, LL,&Hu, HY.(2011).Aggregation of the 35-kDa fragment of TDP-43 causes formation of cytoplasmic inclusions and alteration of RNA processing.FASEB JOURNAL,25(7),2344-2353. |
| MLA | Che, MX,et al."Aggregation of the 35-kDa fragment of TDP-43 causes formation of cytoplasmic inclusions and alteration of RNA processing".FASEB JOURNAL 25.7(2011):2344-2353. |
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