Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly

Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly

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...

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Autores principales: 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
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/a160475f7cbf47d1b2ddb73a38f8b907
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spelling oai:doaj.org-article:a160475f7cbf47d1b2ddb73a38f8b9072021-12-02T17:01:52ZStructural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly10.1038/s41467-019-09902-72041-1723https://doaj.org/article/a160475f7cbf47d1b2ddb73a38f8b9072019-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-09902-7https://doaj.org/toc/2041-1723Low 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.Xinrui GuiFeng LuoYichen LiHeng ZhouZhenheng QinZhenying LiuJinge GuMuyun XieKun ZhaoBin DaiWoo Shik ShinJianhua HeLin HeLin JiangMinglei ZhaoBo SunXueming LiCong LiuDan LiNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
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
Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly
description 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.
format article
author 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
author_facet 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
author_sort Xinrui Gui
title Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly
title_short Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly
title_full Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly
title_fullStr Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly
title_full_unstemmed Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly
title_sort structural basis for reversible amyloids of hnrnpa1 elucidates their role in stress granule assembly
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/a160475f7cbf47d1b2ddb73a38f8b907
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