Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly
文献类型：期刊论文
| 作者 | Gui, XR; Luo, F; Li, YC; Zhou, H; Qin, ZH; Liu, ZY; Gu, JG; Xie, MY; Zhao, K; Dai, B |
| 刊名 | NATURE COMMUNICATIONS
 |
| 出版日期 | 2019 |
| 卷号 | 10期号:-页码:— |
| 关键词 | RNA-BINDING PROTEINS CELL-FREE FORMATION PRION-LIKE DOMAINS PHASE-SEPARATION ATOMIC STRUCTURES BETA-SHEETS STATE FUS TRANSITION MUTATIONS |
| ISSN号 | 2041-1723 |
| DOI | 10.1038/s41467-019-09902-7 |
| 文献子类 | 期刊论文 |
| 英文摘要 | Subcellular membrane-less organelles consist of proteins with low complexity domains. Many of them, such as hnRNPA1, can assemble into both a polydisperse liquid phase and an ordered solid phase of amyloid fibril. The former mirrors biological granule assembly, while the latter is usually associated with neurodegenerative disease. Here, we observe a reversible amyloid formation of hnRNPA1 that synchronizes with liquid-liquid phase separation, regulates the fluidity and mobility of the liquid-like droplets, and facilitates the recruitment of hnRNPA1 into stress granules. We identify the reversible amyloid-forming cores of hnRNPA1 (named hnRACs). The atomic structures of hnRACs reveal a distinct feature of stacking Asp residues, which contributes to fibril reversibility and explains the irreversible pathological fibril formation caused by the Asp mutations identified in familial ALS. Our work characterizes the structural diversity and heterogeneity of reversible amyloid fibrils and illuminates the biological function of reversible amyloid formation in protein phase separation. |
| 语种 | 英语 |
| 源URL | [http://ir.sinap.ac.cn/handle/331007/31829]  |
| 专题 | 上海应用物理研究所_中科院上海应用物理研究所2011-2017年 |
| 作者单位 | 1.Chinese Acad Sci, Shanghai Inst Organ Chem, Interdisciplinary Res Ctr Biol & Chem, Shanghai 201210, Peoples R China; 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China; 3.Shanghai Jiao Tong Univ, Minist Educ, Key Lab Genet Dev & Neuropsychiat Disorders, Bio X Inst, Shanghai, Peoples R China; 4.Tsinghua Univ, Sch Life Sci, Tsinghua Peking Joint Ctr Life Sci, Beijing Adv Innovat Ctr Struct Biol, Beijing, Peoples R China; 5.ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai 201210, Peoples R China; 6.Chinese Acad Sci, Shanghai Inst Appl Phys, 239 Zhang Heng Rd, Shanghai 201203, Peoples R China; 7.Univ Calif Los Angeles, Mol Biol Inst, Dept Neurol, Los Angeles, CA 90095 USA; 8.Univ Calif Los Angeles, Brain Res Inst, Los Angeles, CA 90095 USA; 9.Univ Chicago, Dept Biochem & Mol Biol, Chicago, IL 60637 USA |
| 推荐引用方式 GB/T 7714 | Gui, XR,Luo, F,Li, YC,et al. Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly[J]. NATURE COMMUNICATIONS,2019,10(-):—. |
| APA | Gui, XR.,Luo, F.,Li, YC.,Zhou, H.,Qin, ZH.,...&Li, D.(2019).Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly.NATURE COMMUNICATIONS,10(-),—. |
| MLA | Gui, XR,et al."Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly".NATURE COMMUNICATIONS 10.-(2019):—. |
入库方式： OAI收割
来源：上海应用物理研究所
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