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Article

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

Nature communications - 11 Dec 2020

Sun Yunpeng, Zhao Kun, Xia Wencheng, Feng Guoqin, Gu Jinge, Ma Yeyang, Gui Xinrui, Zhang Xia, Fang Yanshan, Sun Bo, Wang Renxiao, Liu Cong, Li Dan

Abstract excerpt

Human heterogeneous nuclear ribonucleoprotein A1 (hnRNPA1) serves as a key regulating protein in RNA metabolism. Malfunction of hnRNPA1 in nucleo-cytoplasmic transport or dynamic phase separation leads to abnormal amyloid aggregation and neurodegeneration. The low complexity (LC) domain of hnRNPA1 drives both dynamic phase separation and amyloid aggregation. Here, we use cryo-electron microscopy to determine the...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 33311513
DOI: 10.1038/s41467-020-20227-8
PMCID: PMC7733464

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