C9orf72 repeat expansions cause neurodegeneration in Drosophila through arginine-rich proteins
In vitro and in vivo models to dissect repeat RNA and dipeptide repeat protein toxicity are developed, consistent with a dual toxicity mechanism, whereby both arginine-rich proteins and repeat RNA contribute to C9orf72-mediated neurodegeneration.
Ageing as a Risk Factor for Disease
Capu and Spire Assemble a Cytoplasmic Actin Mesh that Maintains Microtubule Organization in the Drosophila Oocyte
Tea3p Is a Cell End Marker Activating Polarized Growth in Schizosaccharomyces pombe
C9orf72 arginine-rich dipeptide proteins interact with ribosomal proteins in vivo to induce a toxic translational arrest that is rescued by eIF1A
expression of the translation initiation factor eIF1A uniquely rescued DPR-induced toxicity in vivo, indicating that restoring translation is a potential therapeutic strategy and directly implicate translational repression in C9orf72 repeat-induced neurodegeneration.
G‐quadruplex‐binding small molecules ameliorate C9orf72 FTD/ALS pathology in vitro and in vivo
Data provide proof of principle that targeting GGGGCC repeat G‐quadruplexes has therapeutic potential and can ameliorate the two key pathologies associated with C9orf72 FTD/ALS.
Sense and antisense RNA are not toxic in Drosophila models of C9orf72-associated ALS/FTD
It is found that neither cytoplasmic nor nuclear sense or antisense RNA are toxic when expressed in adult Drosophila neurons, suggesting they have a limited role in disease pathogenesis.
Ageing as a risk factor for ALS/FTD
Some of the shared mechanisms between the ageing process itself and emerging pathogenic mechanisms in ALS/FTD are highlighted.
RPS25 is required for efficient RAN translation of C9orf72 and other neurodegenerative disease-associated nucleotide repeats
A genetic screen for regulators of RAN translation is performed and small ribosomal protein subunit 25 (RPS25) is identified, presenting a potential therapeutic target for C9orf72-related amyotrophic lateral sclerosis and frontotemporal dementia and other neurodegenerative diseases caused by nucleotide repeat expansions.
The p150-Glued Ssm4p regulates microtubular dynamics and nuclear movement in fission yeast
- Teresa Niccoli, A. Yamashita, P. Nurse, Masayuki Yamamoto
- BiologyJournal of Cell Science
- 1 November 2004
It is shown that Ssm4p, a p150-Glued protein, is induced specifically in response to pheromone and is required for this nuclear movement after cellular and nuclear fusion in the zygote and together with the CLIP-170 homologue Tip1p regulates dynein heavy chain localisation.