bioRxivCell BiologyPreprint
Nuclear transport under stress phenocopies transport defects in models of C9Orf72 ALS
M. F. Semmelink, H. Jafarinia, J. C. Wolters, T. Gheorghe, S. N. Mouton, A. Steen, P. R. Onck, L. M. Veenhoff
Abstract
The nucleus is the hallmark of eukaryotic life and transport to and from the nucleus occurs through the nuclear pore complex (NPC). There is a multitude of data connecting the nuclear transport machinery - i.e. the NPCs and associated nuclear transport factors - to neurodegenerative diseases, but the mechanisms are not well understood. Using Saccharomyces cerevisiae, we systematically studied how the expression of polyPR and polyGA related to C9Orf72 amyotrophic lateral sclerosis impacts the nuclear transport machinery. We measured the abundance and localization of NPC components and transport factors, and assessed the kinetics of import and export by four transport receptors. PolyPR and polyGA cause distinct, and transport receptor dependent effects. We compared the specific changes in transport to those obtained when cells were exposed to different stress situations or mutations. This comparison showed similar patterns of transport defects in cells lacking specific NTRs and cells expressing polyPR. In contrast, polyGA expressing cells bear resemblance to stress conditions where energy maintenance is decreased. The similarity of the patterns of transport deficiencies suggests that polyPR has a direct effect on nuclear transport via NTRs, while polyGA impacts the energy state of the cell and subsequently changes transport.
- organism: yeast
- research focus: cell signaling & trafficking
- research focus: chromatin & epigenetic regulation
- approach: experimental assay
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- C9orf72 polyPR directly binds to various nuclear transport components
H. Jafarinia, E. Van der Giessen, P. Onck·bioRxiv·Jun 22, 2023
- C9ORF72-derived polyGR polypeptides disrupt passive nucleocytoplasmic transport by tuning protein affinity for the nuclear pore barrier
Daniel A. Solomon, Ryan J. Emenecker, … Sarah Mizielinska·bioRxiv·Mar 17, 2026
- Novel single molecule imaging approaches reveal structure-function alterations to the nuclear pore complex in early C9ORF72-associated TDP-43 proteinopathy
Seoungjun Lee, Sarah Mizielinska·bioRxiv·Feb 18, 2026
- C9orf72 poly(PR) mediated neurodegeneration is associated with nucleolar stress
M.E. Cicardi, Justin Hallgren, … Davide Trotti·iSciencePeer-reviewed·Jul 28, 2023
- Modulation of actin polymerization affects nucleocytoplasmic transport in multiple forms of Amyotrophic Lateral Sclerosis
Anthony Giampetruzzi, Eric Danielson, … Claudia Fallini·Nature CommunicationsPeer-reviewed·Aug 23, 2019
- Molecular basis of C9orf72 poly-PR interference with the β-karyopherin family of nuclear transport receptors
H. Jafarinia, E. Van der Giessen, P. R. Onck·bioRxiv·May 5, 2022