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Updated: Jun 25, 2026

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species
Published on: February 27, 2018
Protein aggregation and neurodegeneration: clues from a yeast model of Huntington's disease
N Bocharova1, R Chave-Cox, S Sokolov
1Lomonosov Moscow State University, Russia. bona@genebee.msu.ru
Abstract:
A number of neurodegenerative diseases are accompanied by the appearance of intracellular protein aggregates. Huntington's disease (HD) is caused by a mutation in a gene encoding huntingtin. The mutation causes the expansion of the polyglutamine (polyQ) domain and consequently polyQ-containing aggregates accumulate and neurons in the striatum die. The role of the aggregates is still not clear: they may be the cause of cytotoxicity or a manifestation of the cellular attempt to remove the misfolded proteins. There is accumulating evidence that the main cause of HD is the interaction of the mutated huntingtin with other polyQ-containing proteins and molecular chaperones and most studies based on a yeast model of HD support this point of view. Data obtained using yeasts suggest pathological consequences of polyQ-proteasomal interaction: proteasomal overload by polyQs may interfere with functions of the cell cycle-regulating proteins.
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