Cargando…
Phosphorylation of the FUS low‐complexity domain disrupts phase separation, aggregation, and toxicity
Neuronal inclusions of aggregated RNA‐binding protein fused in sarcoma (FUS) are hallmarks of ALS and frontotemporal dementia subtypes. Intriguingly, FUS's nearly uncharged, aggregation‐prone, yeast prion‐like, low sequence‐complexity domain (LC) is known to be targeted for phosphorylation. Her...
Autores principales: | Monahan, Zachary, Ryan, Veronica H, Janke, Abigail M, Burke, Kathleen A, Rhoads, Shannon N, Zerze, Gül H, O'Meally, Robert, Dignon, Gregory L, Conicella, Alexander E, Zheng, Wenwei, Best, Robert B, Cole, Robert N, Mittal, Jeetain, Shewmaker, Frank, Fawzi, Nicolas L |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5641905/ https://www.ncbi.nlm.nih.gov/pubmed/28790177 http://dx.doi.org/10.15252/embj.201696394 |
Ejemplares similares
-
Molecular interactions underlying liquid-liquid phase separation of the FUS low complexity domain
por: Murthy, Anastasia C., et al.
Publicado: (2019) -
The prionlike domain of FUS is multiphosphorylated following DNA damage without altering nuclear localization
por: Rhoads, Shannon N., et al.
Publicado: (2018) -
The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS
por: Rhoads, Shannon N., et al.
Publicado: (2018) -
TDP-43 α-helical structure tunes liquid–liquid phase separation and function
por: Conicella, Alexander E., et al.
Publicado: (2020) -
Proteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates
por: Wear, Maggie P., et al.
Publicado: (2015)