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Huntington’s disease mutations lead to expansion of a polyglutamine (polyQ) sequence in Httex1 to lengths longer than 36Q, whereas the wild-sort protein is often lower than 25Q ( Duyao et al., 1993 ). PolyQ-expansion causes Httex1 to change into extremely aggregation prone, which manifests as intracellular inclusion our bodies as the illness progresses ( Davies et al., 1997 ; DiFiglia et al., 1997 ; Scherzinger et al., 1997 ). We and others have used transient expression constructs of Httex1 fused to fluorescent proteins as models for replicating essential features of the illness, including protein homeostasis stress ( Arrasate et al., 2004 ; Hosp et al., 2017 ; Kim et al., 2016 ; Moily et al., 2017 ; Ramdzan et al., 2017 ). Mutant Httex1-fluorescent protein constructs progressively type massive cytosolic inclusions in cell culture over time.

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