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Biochemistry (Mosc). 2009 Feb;74(2):231-4.

Protein aggregation and neurodegeneration: clues from a yeast model of Huntington's disease.

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1
Lomonosov 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.

PMID:
19267681
[Indexed for MEDLINE]
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