Acetylation Disfavors Tau Phase Separation

• Published in: International journal of molecular sciences Vol. 19; no. 5; p. 1360
• Main Authors: Ferreon, Josephine C, Jain, Antrix, Choi, Kyoung-Jae, Tsoi, Phoebe S, MacKenzie, Kevin R, Jung, Sung Yun, Ferreon, Allan Chris
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 04.05.2018; MDPI
• Subjects: Acetylation; Amyloidogenesis; Biocompatibility; Chromatin; Deoxyribonucleic acid; DNA; DNA-binding protein; Event-related potentials; FUS protein; Heparin; Histone acetyltransferase; intrinsically disordered protein; membrane-less organelle; neurodegenerative disease; p300 HAT acetylation; Phase separation; Phosphorylation; post-translational modification; protein aggregation; Proteins; Sarcoma; Tau fibrillation; Tau protein; intrinsically disordered protein; neurodegenerative disease; p300 HAT acetylation; protein aggregation; Tau fibrillation; post-translational modification; membrane-less organelle

Neuropathological aggregates of the intrinsically disordered microtubule-associated protein Tau are hallmarks of Alzheimer's disease, with decades of research devoted to studying the protein's aggregation properties both in vitro and in vivo. Recent demonstrations that Tau is capable of un...