Nature Communications (May 2019)
Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly
- Xinrui Gui,
- Feng Luo,
- Yichen Li,
- Heng Zhou,
- Zhenheng Qin,
- Zhenying Liu,
- Jinge Gu,
- Muyun Xie,
- Kun Zhao,
- Bin Dai,
- Woo Shik Shin,
- Jianhua He,
- Lin He,
- Lin Jiang,
- Minglei Zhao,
- Bo Sun,
- Xueming Li,
- Cong Liu,
- Dan Li
Affiliations
- Xinrui Gui
- Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences
- Feng Luo
- Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences
- Yichen Li
- Bio-X Institutes, Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders, Ministry of Education, Shanghai Jiao Tong University
- Heng Zhou
- Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University
- Zhenheng Qin
- School of Life Science and Technology, ShanghaiTech University
- Zhenying Liu
- Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences
- Jinge Gu
- Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences
- Muyun Xie
- Shanghai Institute of Applied Physics, Chinese Academy of Sciences
- Kun Zhao
- Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences
- Bin Dai
- Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences
- Woo Shik Shin
- Department of Neurology, Molecular Biology Institute, and Brain Research Institute, UCLA
- Jianhua He
- Shanghai Institute of Applied Physics, Chinese Academy of Sciences
- Lin He
- Bio-X Institutes, Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders, Ministry of Education, Shanghai Jiao Tong University
- Lin Jiang
- Department of Neurology, Molecular Biology Institute, and Brain Research Institute, UCLA
- Minglei Zhao
- Department of Biochemistry and Molecular Biology, the University of Chicago
- Bo Sun
- School of Life Science and Technology, ShanghaiTech University
- Xueming Li
- Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University
- Cong Liu
- Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences
- Dan Li
- Bio-X Institutes, Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders, Ministry of Education, Shanghai Jiao Tong University
- DOI
- https://doi.org/10.1038/s41467-019-09902-7
- Journal volume & issue
-
Vol. 10,
no. 1
pp. 1 – 12
Abstract
Low complexity (LC) domains can drive the formation of both amyloid fibrils and protein droplets. Here, the authors identify reversible amyloid cores from the LC of hnRNPA1, based on which they elucidate the structural basis of reversible fibrillation and its interplay with hnRNPA1 droplet formation.
