The prionlike domain of FUS is multiphosphorylated following DNA damage without altering nuclear localization.

ABSTRACT: 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 increased cytoplasmic localization are both hypothesized to predispose FUS to irreversible aggregation, which is a pathological hallmark of subtypes of amyotrophic lateral sclerosis and frontotemporal dementia. We previously showed that phosphorylation of FUS's prionlike domain suppressed phase separation and toxic aggregation, proportionally to the number of added phosphates. However, phosphorylation of FUS's prionlike domain was previously reported to promote its cytoplasmic localization, potentiall

SUBMITTER: Rhoads SN 

PROVIDER: S-EPMC6085830 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature