Acetylation of intrinsically disordered regions regulates phase separation

• Published in: Nature chemical biology Vol. 15; no. 1; pp. 51 - 61
• Main Authors: Saito, Makoto, Hess, Daniel, Eglinger, Jan, Fritsch, Anatol W., Kreysing, Moritz, Weinert, Brian T., Choudhary, Chunaram, Matthias, Patrick
• Format: Journal Article
• Language: English
• Published: New York Nature Publishing Group US 01.01.2019; Nature Publishing Group
• Subjects: 631/45; 631/80; 631/92/458; 631/92/475; Acetylation; Amyotrophic lateral sclerosis; Animals; Biochemical Engineering; Biochemistry; Biology; Bioorganic Chemistry; Catalytic Domain; Cell Biology; Chemistry; Chemistry and Materials Science; Chemistry/Food Science; Cytoplasmic Granules - metabolism; Deacetylation; DEAD-box RNA Helicases - metabolism; DNA helicase; Gene Knockout Techniques; Histone Deacetylase 6 - metabolism; Humans; Intrinsically Disordered Proteins - chemistry; Intrinsically Disordered Proteins - metabolism; Liquid phases; Lysine; Lysine - metabolism; Mice; Models, Theoretical; Mutation; Organelles; Osmotic Pressure; Phase separation; Proteins; Ribonucleic acid; RNA; RNA helicase; RNA Helicases - chemistry; RNA Helicases - genetics; RNA Helicases - metabolism; Substrates

Liquid–liquid phase separation (LLPS) of proteins containing intrinsically disordered regions (IDRs) has been proposed as a mechanism underlying the formation of membrane-less organelles. Tight regulation of IDR behavior is essential to ensure that LLPS only takes place when necessary. Here, we repo...