Cargando…
The prionlike domain of FUS is multiphosphorylated following DNA damage without altering nuclear localization
FUS (fused in sarcoma) is an abundant, predominantly nuclear protein involved in RNA processing. Under various conditions, FUS functionally associates with RNA and other macromolecules to form distinct, reversible phase-separated liquid structures. Persistence of the phase-separated state and increa...
Autores principales: | Rhoads, Shannon N., Monahan, Zachary T., Yee, Debra S., Leung, Andrew Y., Newcombe, Cameron G., O’Meally, Robert N., Cole, Robert N., Shewmaker, Frank P. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6085830/ https://www.ncbi.nlm.nih.gov/pubmed/29897835 http://dx.doi.org/10.1091/mbc.E17-12-0735 |
Ejemplares similares
-
The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS
por: Rhoads, Shannon N., et al.
Publicado: (2018) -
Phosphorylation of the FUS low‐complexity domain disrupts phase separation, aggregation, and toxicity
por: Monahan, Zachary, et al.
Publicado: (2017) -
Yeast Models of Prion-Like Proteins That Cause Amyotrophic Lateral Sclerosis Reveal Pathogenic Mechanisms
por: Monahan, Zachary T., et al.
Publicado: (2018) -
Proteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates
por: Wear, Maggie P., et al.
Publicado: (2015) -
Accelerated Multiphosphorylated
Peptide Synthesis
por: Grunhaus, Dana, et al.
Publicado: (2022)