Nature Communications (Sep 2019)

The mutational landscape of a prion-like domain

  • Benedetta Bolognesi,
  • Andre J. Faure,
  • Mireia Seuma,
  • Jörn M. Schmiedel,
  • Gian Gaetano Tartaglia,
  • Ben Lehner

DOI
https://doi.org/10.1038/s41467-019-12101-z
Journal volume & issue
Vol. 10, no. 1
pp. 1 – 12

Abstract

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TDP43 aggregates are a hallmark of amyotrophic lateral sclerosis. By using deep mutagenesis to measure the toxicity of more than 50,000 mutations in the prion domain of TDP43, the authors conclude that mutations that increase toxicity promote formation of liquid-like condensates, while aggregation of TDP43 is protective for the cell.