Aggregation of scaffolding protein DISC1 dysregulates phosphodiesterase 4 in Huntington’s disease

• Published in: The Journal of clinical investigation Vol. 127; no. 4; pp. 1438 - 1450
• Main Authors: Tanaka, Motomasa, Ishizuka, Koko, Nekooki-Machida, Yoko, Endo, Ryo, Takashima, Noriko, Sasaki, Hideyuki, Komi, Yusuke, Gathercole, Amy, Huston, Elaine, Ishii, Kazuhiro, Hui, Kelvin Kai-Wan, Kurosawa, Masaru, Kim, Sun-Hong, Nukina, Nobuyuki, Takimoto, Eiki, Houslay, Miles D., Sawa, Akira
• Format: Journal Article
• Language: English
• Published: United States American Society for Clinical Investigation 01.04.2017
• Subjects: Animals; Behavior; Biomedical research; Brain research; Care and treatment; Cellular proteins; Cyclic Nucleotide Phosphodiesterases, Type 4 - metabolism; Development and progression; Experiments; Female; Gene expression; Genetic aspects; Health aspects; HEK293 Cells; Humans; Huntingtin Protein - genetics; Huntingtin Protein - metabolism; Huntington Disease - enzymology; Huntington's disease; Huntingtons disease; Mice, Transgenic; Mutation; Nerve Tissue Proteins - metabolism; Pathology; Phosphodiesterases; Protein Aggregation, Pathological - enzymology; Proteins; Scientists; Studies

Huntington's disease (HD) is a polyglutamine (polyQ) disease caused by aberrant expansion of the polyQ tract in Huntingtin (HTT). While motor impairment mediated by polyQ-expanded HTT has been intensively studied, molecular mechanisms for nonmotor symptoms in HD, such as psychiatric manifestati...