Article
The dystonia-associated Torsin1A sustains CLCC1 function in membrane fusion of the nuclear envelope for NPC biogenesis.
Molecular cell - 3 Sept 2026
Maslennikova Daria, Baird Harry, Ding Xinyue, Kumar Ashutosh, Loffreda Alessia, Ramachandran Kausthubh, Kösters Benjamin Jonas, Bos Jelmi Uit de, Ashiono Caroline, Frischer-Ordu Katharina, Luithle Naemi, Uliana Federico, Dey Gautam, Korkhov Volodymyr M, Antonin Wolfram, Vanni Stefano, Jagannathan Madhav, Kutay Ulrike
Abstract excerpt
DYT1 dystonia is an incurable movement disorder caused by a loss-of-function mutation in Torsin1A, an endoplasmic reticulum (ER)-resident AAA+ ATPase. Here, we use Drosophila and human cells to shed light on Torsins' mode of action. Fly germ cells lacking dTorsin arrest in development with defects in nuclear pore complex (NPC) biogenesis due to impaired nuclear envelope membrane fusion. We identify the conserved...
Read the complete abstract on PubMedTopics
- Animals
- Molecular Chaperones
- Nuclear Envelope
- Humans
- Drosophila Proteins