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 language | English |
|---|---|
| Pages (from-to) | 339-357.e7 |
| Journal | Neuron |
| Volume | 102 |
| Issue number | 2 |
| DOIs | |
| State | Published - 17 Apr 2019 |
| Externally published | Yes |
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
All Science Journal Classification (ASJC) codes
- General Neuroscience