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Updated: Feb 23, 2026

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species
Published on: February 27, 2018
A toxic mutant huntingtin species is resistant to selective autophagy
Yuhua Fu1, Peng Wu1, Yuyin Pan1
1State Key Laboratory of Medical Neurobiology, Neurology Department at Huashan Hospital, School of Life Sciences, Fudan University, Shanghai, China.
Abstract:
Protein misfolding is a common theme in neurodegenerative disorders including Huntington's disease (HD). The HD-causing mutant huntingtin protein (mHTT) has an expanded polyglutamine (polyQ) stretch that may adopt multiple conformations, and the most toxic of these is the one recognized by antibody 3B5H10. Here we show that the 3B5H10-recognized mHTT species has a slower degradation rate due to its resistance to selective autophagy in human cells and brains, revealing mechanisms of its higher toxicity.
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