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

Subcellular mislocalization and aggregation of the human FUS protein occurs in neurons of patients with subtypes of amyotrophic lateral sclerosis and frontotemporal dementia. FUS is one of several RNA-binding proteins that can functionally self-associate into distinct liquid-phase droplet structures. It is postulated that aberrant interactions within the dense phase-separated state can potentiate FUS’s transition into solid prion-like aggregates that cause disease. FUS is post-translationally modified at numerous positions, which affect both its localization and aggregation propensity. These modifications may influence FUS-linked pathology and serve as therapeutic targets.

• Publication year

  2018

• Venue

  International Journal of Molecular Sciences

• Publication date

  2018-03-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.3390/ijms19030886PMID 29547565PMCID 5877747
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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