Article
Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation-Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6.
Angewandte Chemie (International ed. in English) - 2 May 2017
Chiki Anass, DeGuire Sean M, Ruggeri Francesco S, Sanfelice Domenico, Ansaloni Annalisa, Wang Zhe-Ming, Cendrowska Urszula, Burai Ritwik, Vieweg Sophie, Pastore Annalisa, Dietler Giovanni, Lashuel Hilal A
Abstract excerpt
Herein, we used protein semisynthesis to investigate, for the first time, the effect of lysine acetylation and phosphorylation, as well as the crosstalk between these modifications on the structure and aggregation of mutant huntingtin exon1 (Httex1). Our results demonstrate that phosphorylation at T3 stabilizes the α-helical conformation of the N-terminal 17 amino acids (Nt17) and significantly inhibits the...
Topics
- Acetylation
- Exons
- Humans
- Huntingtin Protein
- Mutation
- Phosphorylation
- Protein Aggregates
- Protein Conformation
- Protein Processing, Post-Translational