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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Bibliographic Details
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
Description
Summary: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.
ISSN:2041-1723

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