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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Main Authors:	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
Format:	Article
Language:	English
Published:	Nature Publishing Group 2020-12-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-020-20227-8

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spelling	doaj-7fbc850f6f3e46a78b4dbc0a94ba0a022021-01-31T12:50:09ZengNature Publishing GroupNature Communications2041-17232020-12-011111810.1038/s41467-020-20227-8The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structureYunpeng Sun0Kun Zhao1Wencheng Xia2Guoqin Feng3Jinge Gu4Yeyang Ma5Xinrui Gui6Xia Zhang7Yanshan Fang8Bo Sun9Renxiao Wang10Cong Liu11Dan Li12Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of SciencesInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of SciencesInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of SciencesUniversity of Chinese Academy of SciencesInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of SciencesInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of SciencesInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of SciencesSchool of Life Science and Technology, ShanghaiTech UniversityInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of SciencesSchool of Life Science and Technology, ShanghaiTech UniversityUniversity of Chinese Academy of SciencesInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of SciencesBio-X-Renji Hospital Research Center, Renji Hospital, School of Medicine, Shanghai Jiao Tong UniversityHeterogeneous 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.https://doi.org/10.1038/s41467-020-20227-8
collection	DOAJ
language	English
format	Article
sources	DOAJ
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
spellingShingle	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 Nature Communications
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 Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2020-12-01
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.
url	https://doi.org/10.1038/s41467-020-20227-8
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The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure

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