Cytoplasmic TDP-43 De-mixing Independent of Stress Granules Drives Inhibition of Nuclear Import, Loss of Nuclear TDP-43, and Cell Death

Fatima Gasset-Rosa, Shan Lu, Haiyang Yu, Cong Chen, Ze'ev Melamed, Lin Guo, James Shorter, Sandrine Da Cruz*, Don W. Cleveland

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

281 Scopus citations

Abstract

TDP-43 aggregation is the major hallmark of multiple neurodegenerative diseases, including ALS and FTD. Gasset-Rosa et al. demonstrate that transient stress induces long-lasting cytoplasmic TDP-43 de-mixing independent of stress granules, driving nuclear import defects, nuclear TDP-43 clearance, and cell death.

Original languageAmerican English
Pages (from-to)339-357.e7
JournalNeuron
Volume102
Issue number2
DOIs
StatePublished - 17 Apr 2019
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2019 Elsevier Inc.

Keywords

  • ALS/FTD
  • RNA-binding proteins
  • TDP-43
  • TDP-43 de-mixing
  • iPSCs
  • liquid-liquid phase separation
  • low complexity domains
  • motor neurons
  • neurodegeneration
  • nucleocytoplasmic transport
  • stress granules

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