Implications of the Orb2 Amyloid Structure in Huntington’s Disease

International Journal of Molecular Sciences

AlexeyG. Murzin¹  Kausik Si²  Rubén Hervás² 

[1] MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK;Stowers Institute for Medical Research, Kansas City, MO 64110, USA;

关键词: functional amyloids;    CPEB;    Orb2;    huntingtin;    Huntington’s disease;    polyglutamine;   

DOI  :  10.3390/ijms21186910

来源: DOAJ

【 摘 要 】

Huntington’s disease is a progressive, autosomal dominant, neurodegenerative disorder caused by an expanded CAG repeat in the huntingtin gene. As a result, the translated protein, huntingtin, contains an abnormally long polyglutamine stretch that makes it prone to misfold and aggregating. Aggregation of huntingtin is believed to be the cause of Huntington’s disease. However, understanding on how, and why, huntingtin aggregates are deleterious has been hampered by lack of enough relevant structural data. In this review, we discuss our recent findings on a glutamine-based functional amyloid isolated from Drosophila brain and how this information provides plausible structural insight on the structure of huntingtin deposits in the brain.

【 授权许可】

Unknown