Nature Communications (May 2019)

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

  • 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

DOI
https://doi.org/10.1038/s41467-019-09902-7
Journal volume & issue
Vol. 10, no. 1
pp. 1 – 12

Abstract

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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.