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Updated: Dec 14, 2025

Assays for the Degradation of Misfolded Proteins in Cells
Published on: August 28, 2016
Autophagy and Polyglutamine Disease
Haigang Ren1, Zongbing Hao1, Guanghui Wang2
1Laboratory of Molecular Neuropathology, Jiangsu Key Laboratory of Neuropsychiatric Diseases, Department of Pharmacology, College of Pharmaceutical Sciences, Soochow University, Suzhou, 215123, Jiangsu, China.
Abstract:
Polyglutamine (polyQ) disease is a type of fatal neurodegenerative disease caused by an expansion of CAG repeats in a specific gene, resulting in a protein with an abnormal polyQ fragment. The age of onset and the degree of pathological deterioration are related to the length of the polyQ fragment. At least 9 kinds of polyglutamine diseases have been discovered, including Huntington disease (HD), dentatorubral pallidoluysian atrophy (DRPLA), spinobulbar muscular atrophy (SBMA) and six spinocerebellar ataxia (SCA) such as SCA1, 2, 3, 6, 7 and 17 subtypes (Table 9.1). Previous studies suggest that autophagy plays a major role in the quality control of disease proteins in polyQ diseases. In this chapter, we majorly focused on three representative polyQ diseases, including spinocerebellar Ataxia type 3 (SCA3), spinocerebellar ataxia type 7 (SCA7) and Huntington's disease (HD). The relationship of the ubiquitin-proteasome system and autophagy involved in disease protein accumulation were summarized.
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