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Identification of an RNA Polymerase III Regulator Linked to Disease-Associated Protein Aggregation.

Molecular cell | Mar 16, 2017

Protein aggregation is associated with age-related neurodegenerative disorders, such as Alzheimer's and polyglutamine diseases. As a causal relationship between protein aggregation and neurodegeneration remains elusive, understanding the cellular mechanisms regulating protein aggregation will help develop future treatments. To identify such mechanisms, we conducted a forward genetic screen in a C. elegans model of polyglutamine aggregation and identified the protein MOAG-2/LIR-3 as a driver of protein aggregation. In the absence of polyglutamine, MOAG-2/LIR-3 regulates the RNA polymerase III-associated transcription of small non-coding RNAs. This regulation is lost in the presence of polyglutamine, which mislocalizes MOAG-2/LIR-3 from the nucleus to the cytosol. We then show biochemically that MOAG-2/LIR-3 can also catalyze the aggregation of polyglutamine-expanded huntingtin. These results suggest that polyglutamine can induce an aggregation-promoting activity of MOAG-2/LIR-3 in the cytosol. The concept that certain aggregation-prone proteins can convert other endogenous proteins into drivers of aggregation and toxicity adds to the understanding of how cellular homeostasis can be deteriorated in protein misfolding diseases.

Pubmed ID: 28306505 RIS Download

Mesh terms: Active Transport, Cell Nucleus | Animals | Animals, Genetically Modified | Binding Sites | Caenorhabditis elegans | Caenorhabditis elegans Proteins | Cell Nucleus | Cytosol | Disease Models, Animal | Neurodegenerative Diseases | Peptides | Promoter Regions, Genetic | Protein Aggregates | Protein Aggregation, Pathological | Protein Binding | RNA Interference | RNA Polymerase III | RNA, Small Untranslated | Transcription Factors | Transcription, Genetic

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