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  3. Nuclear Export Modulates Tdp-43 Phase Transition And Cytoplasmic Aggregation.
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  3. Nuclear Export Modulates Tdp-43 Phase Transition And Cytoplasmic Aggregation.

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Nuclear export modulates TDP-43 phase transition and cytoplasmic aggregation.

Natalie Chin1, Qi Zhang2, Jizhong Zou3

  • 1Laboratory of Molecular Biology, National Institute of Diabetes, Digestive, and Kidney Diseases, National Institutes of Health, Bethesda, MD, 20892, USA.

Biorxiv : the Preprint Server for Biology
|April 17, 2026

View abstract on PubMed

Summary
This summary is machine-generated.

Cellular factors regulate the phase behavior of TAR DNA-binding protein 43 (TDP-43), a key protein implicated in neurodegenerative diseases like ALS. Inhibiting nuclear export promotes TDP-43 liquid-like states, reducing harmful aggregation.

Keywords:
Amyotrophic Lateral Sclerosis (ALS)Frontotemporal Dementia (FTD)TDP-43XPO1anisosomeliquid-liquid phase separation/LLPSnuclear transportprotein aggregation

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Area of Science:

  • Neurobiology
  • Molecular Biology
  • Biochemistry

Background:

  • TAR DNA-binding protein 43 (TDP-43) forms nuclear liquid-like assemblies, influencing its aggregation and neurotoxicity.
  • The mechanisms controlling TDP-43's liquid-to-solid phase transition are not well understood.

Purpose of the Study:

  • To identify cellular factors modulating TDP-43 phase behavior, particularly in an Amyotrophic Lateral Sclerosis (ALS)-associated mutant.
  • To elucidate the role of nuclear export in regulating TDP-43 phase transitions and aggregation.

Main Methods:

  • Chemical and genome-wide genetic screens were employed to identify TDP-43 phase regulators.
  • An in vitro semi-permeabilized cell system was used to dynamically recapitulate TDP-43 phase transitions.
  • Brain organoid models with ALS-associated mutations were utilized for validation.

Main Results:

  • RNA splicing, protein translation, proteostasis, and nuclear export were identified as key TDP-43 phase regulators.
  • Inhibition of nuclear export favors an RNA-dependent TDP-43 liquid-liquid phase separation (LLPS) state in vitro.
  • Nuclear export deficiency was shown to limit pathogenic phospho-TDP-43 accumulation in ALS brain organoids.

Conclusions:

  • Nuclear export is a critical regulator of TDP-43 phase transitions.
  • A mechanistic framework links altered nuclear transport and phase dynamics to TDP-43 aggregation potential in neurodegeneration.