Article

The Low Complexity Domain of the FUS RNA Binding Protein Self-assembles via the Mutually Exclusive Use of Two Distinct Cross-β Cores

2021-08-05

Abstract excerpt

The low complexity (LC) domain of the fused in sarcoma (FUS) RNA binding protein self-associates in a manner causing phase separation from an aqueous environment. Incubation of the FUS LC domain under physiologically normal conditions of salt and pH leads to rapid formation of liquid-like droplets that mature into a gel-like state. Both examples of phase separation have enabled reductionist biochemical assays allo...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: fc115753-c113-543d-a0a6-9a50c63e3056
DOI: 10.1101/2021.08.05.455316

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

The Low Complexity Domain of the FUS RNA Binding Protein Self-assembles via the Mutually Exclusive Use of Two Distinct Cross-β CoresDOI 10.1101/2021.08.05.455316Read

Breaking β-sheets in FUS prion-like domain preserves phase separation and function but prevents aggregation and toxicitySemantic proximity Read

Fused in Sarcoma: Properties, Self-Assembly and Correlation with Neurodegenerative DiseasesSemantic proximity Read

ALS/FTLD-Linked Mutations in FUS Glycine Residues Cause Accelerated Gelation and Reduced Interactions with Wild-Type FUS.Semantic proximity Read

A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation.Semantic proximity Read

Real-Time Observation of Structure and Dynamics during the Liquid-to-Solid Transition of FUS LCSemantic proximity Read

HspB8 prevents aberrant phase transitions of FUS by chaperoning its folded RNA binding domainSemantic proximity Read

HspB8 prevents aberrant phase transitions of FUS by chaperoning its folded RNA-binding domain.Semantic proximity Read

The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS.Semantic proximity Read

The physiological and pathological biophysics of phase separation and gelation of RNA binding proteins in amyotrophic lateral sclerosis and fronto-temporal lobar degeneration.Semantic proximity Read

The phase separation-dependent FUS interactome reveals nuclear and cytoplasmic function of liquid–liquid phase separationSemantic proximity Read

Atomic structures of FUS LC domain segments reveal bases for reversible amyloid fibril formation.Semantic proximity Read

Toxic PR poly-dipeptides encoded by the <i>C9orf72</i> repeat expansion target Kapβ2 and dysregulate phase separation of low-complexity domainsSemantic proximity Read