Huntingtin facilitates polycomb repressive complex 2

• Published in: Human molecular genetics Vol. 19; no. 4; pp. 573 - 583
• Main Authors: Seong, Ihn Sik, Woda, Juliana M., Song, Ji-Joon, Lloret, Alejandro, Abeyrathne, Priyanka D., Woo, Caroline J., Gregory, Gillian, Lee, Jong-Min, Wheeler, Vanessa C., Walz, Thomas, Kingston, Robert E., Gusella, James F., Conlon, Ronald A., MacDonald, Marcy E.
• Format: Journal Article
• Language: English
• Published: Oxford Oxford University Press 15.02.2010
• Subjects: Animals; Biological and medical sciences; Disease Models, Animal; Female; Fundamental and applied biological sciences. Psychology; Genetics of eukaryotes. Biological and molecular evolution; Histones - genetics; Histones - metabolism; Humans; Huntingtin Protein; Huntington Disease - embryology; Huntington Disease - genetics; Huntington Disease - metabolism; Male; Mice; Mice, Knockout; Molecular and cellular biology; Molecular Sequence Data; Nerve Tissue Proteins - chemistry; Nerve Tissue Proteins - genetics; Nerve Tissue Proteins - metabolism; Nuclear Proteins - chemistry; Nuclear Proteins - genetics; Nuclear Proteins - metabolism; Polycomb-Group Proteins; Protein Binding; Repressor Proteins - genetics; Repressor Proteins - metabolism; Sequence Homology, Amino Acid; Huntingtin; Genetics

Huntington's disease (HD) is caused by expansion of the polymorphic polyglutamine segment in the huntingtin protein. Full-length huntingtin is thought to be a predominant HEAT repeat α-solenoid, implying a role as a facilitator of macromolecular complexes. Here we have investigated huntingtin&#...