Impaired RNA Binding Does Not Prevent Histone Modification Changes in a FUS ALS/FTD Yeast Model.

Mutations in the RNA-binding protein FUS are linked to amyotrophic lateral sclerosis and frontotemporal dementia (ALS/FTD). FUS mutants mislocalize and aggregate in dying neurons. We previously established that FUS proteinopathy is linked to changes in the histone modification landscape in a yeast ALS/FTD model.

[PRION] States Are Associated with Specific Histone H3 Post-Translational Modification Changes.

Prions are proteins able to take on alternative conformations and propagate them in a self-templating process. In , prions enable heritable responses to environmental conditions through bet-hedging mechanisms. Hence, [PRION] states may serve as an atypical form of epigenetic control, producing heritable phenotypic change via protein folding.

Trichostatin A Relieves Growth Suppression and Restores Histone Acetylation at Specific Sites in a FUS ALS/FTD Yeast Model.

Amyotrophic lateral sclerosis (ALS) is an incurable neurodegenerative disease that often occurs concurrently with frontotemporal dementia (FTD), another disorder involving progressive neuronal loss. ALS and FTD form a neurodegenerative continuum and share pathological and genetic features. Mutations in a multitude of genes have been linked to ALS/FTD, including The FUS protein aggregates and forms inclusions within affected neurons.