The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure

The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure

Heterogeneous nuclear ribonucleoprotein A1 (hnRNPA1) shuttles between the nucleus and cytoplasm to regulate gene expression and RNA metabolism and its low complexity (LC) C-terminal domain facilitates liquid–liquid phase separation and amyloid aggregation. Here, the authors present the cryo-EM struc...

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Autores principales: Yunpeng Sun, Kun Zhao, Wencheng Xia, Guoqin Feng, Jinge Gu, Yeyang Ma, Xinrui Gui, Xia Zhang, Yanshan Fang, Bo Sun, Renxiao Wang, Cong Liu, Dan Li
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/7fbc850f6f3e46a78b4dbc0a94ba0a02
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spelling oai:doaj.org-article:7fbc850f6f3e46a78b4dbc0a94ba0a022021-12-02T13:24:05ZThe nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure10.1038/s41467-020-20227-82041-1723https://doaj.org/article/7fbc850f6f3e46a78b4dbc0a94ba0a022020-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20227-8https://doaj.org/toc/2041-1723Heterogeneous nuclear ribonucleoprotein A1 (hnRNPA1) shuttles between the nucleus and cytoplasm to regulate gene expression and RNA metabolism and its low complexity (LC) C-terminal domain facilitates liquid–liquid phase separation and amyloid aggregation. Here, the authors present the cryo-EM structure of amyloid fibrils formed by the hnRNPA1 LC domain, which reveals that the hnRNPA1 nuclear localization sequence forms the fibril core, and they discuss how ALS-causing mutations affect fibril stability.Yunpeng SunKun ZhaoWencheng XiaGuoqin FengJinge GuYeyang MaXinrui GuiXia ZhangYanshan FangBo SunRenxiao WangCong LiuDan LiNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-8 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Yunpeng Sun
Kun Zhao
Wencheng Xia
Guoqin Feng
Jinge Gu
Yeyang Ma
Xinrui Gui
Xia Zhang
Yanshan Fang
Bo Sun
Renxiao Wang
Cong Liu
Dan Li
The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure
description Heterogeneous nuclear ribonucleoprotein A1 (hnRNPA1) shuttles between the nucleus and cytoplasm to regulate gene expression and RNA metabolism and its low complexity (LC) C-terminal domain facilitates liquid–liquid phase separation and amyloid aggregation. Here, the authors present the cryo-EM structure of amyloid fibrils formed by the hnRNPA1 LC domain, which reveals that the hnRNPA1 nuclear localization sequence forms the fibril core, and they discuss how ALS-causing mutations affect fibril stability.
format article
author Yunpeng Sun
Kun Zhao
Wencheng Xia
Guoqin Feng
Jinge Gu
Yeyang Ma
Xinrui Gui
Xia Zhang
Yanshan Fang
Bo Sun
Renxiao Wang
Cong Liu
Dan Li
author_facet Yunpeng Sun
Kun Zhao
Wencheng Xia
Guoqin Feng
Jinge Gu
Yeyang Ma
Xinrui Gui
Xia Zhang
Yanshan Fang
Bo Sun
Renxiao Wang
Cong Liu
Dan Li
author_sort Yunpeng Sun
title The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure
title_short The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure
title_full The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure
title_fullStr The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure
title_full_unstemmed The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure
title_sort nuclear localization sequence mediates hnrnpa1 amyloid fibril formation revealed by cryoem structure
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/7fbc850f6f3e46a78b4dbc0a94ba0a02
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