Expanded Polyglutamine-containing N-terminal Huntingtin Fragments Are Entirely Degraded by Mammalian Proteasomes

• Published in: The Journal of biological chemistry Vol. 288; no. 38; pp. 27068 - 27084
• Main Authors: Juenemann, Katrin, Schipper-Krom, Sabine, Wiemhoefer, Anne, Kloss, Alexander, Sanz Sanz, Alicia, Reits, Eric A.J.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 20.09.2013; American Society for Biochemistry and Molecular Biology
• Subjects: Aggregation; Animals; Autophagy; Cell Line; Humans; Huntingtin Protein; Huntington Disease; Mice; Mice, Knockout; Molecular Bases of Disease; Nerve Tissue Proteins - genetics; Nerve Tissue Proteins - metabolism; Nuclear Proteins - genetics; Nuclear Proteins - metabolism; Peptides - genetics; Peptides - metabolism; Polyglutamine; Proteasome; Proteasome Endopeptidase Complex - genetics; Proteasome Endopeptidase Complex - metabolism; Proteolysis; Repetitive Sequences, Amino Acid; Aggregation; Huntington Disease; Polyglutamine; Autophagy; Proteasome

Huntington disease is a neurodegenerative disorder caused by an expanded polyglutamine (polyQ) repeat within the protein huntingtin (Htt). N-terminal fragments of the mutant Htt (mHtt) proteins containing the polyQ repeat are aggregation-prone and form intracellular inclusion bodies. Improving the c...