The discovery of a causative link between dysfunction of a number of RNA-binding proteins with prion-like domains and the development of certain (neuro)degenerative diseases has completely changed our perception of molecular mechanisms instigating pathological process in these disorders. Irreversible aggregation of these proteins is a crucial pathogenic event delineating a type of proteinopathy. FUS (fused in sarcoma) is a prototypical member of the class, and studies into the causes and consequences of FUSopathies have been instrumental in characterizing the processes leading to deregulation of RNA metabolism in neurodegeneration. In vivo models of FUSopathy have provided critical insights into the mechanisms of FUS toxicity and clues on the role of non-amyloid aggregates, which are hallmarks of these diseases. The present review summarizes the data on FUS aggregation signatures in available model organisms on the basis of overexpression of FUS variants.
Conference Article| November 20 2013
Modelling FUSopathies: focus on protein aggregation
Tatyana A. Shelkovnikova
Tatyana A. Shelkovnikova 1
*School of Biosciences, Cardiff University, Museum Avenue, Cardiff CF10 3AX, U.K.
†Institute of Physiologically Active Compounds, Russian Academy of Sciences, 1 Severniy proezd, Chernogolovka 142432, Moscow Region, Russia
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Tatyana A. Shelkovnikova; Modelling FUSopathies: focus on protein aggregation. Biochem Soc Trans 1 December 2013; 41 (6): 1613–1617. doi: https://doi.org/10.1042/BST20130212
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