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Article

ALS mutations in the TIA-1 prion-like domain trigger highly condensed pathogenic structures.

Proceedings of the National Academy of Sciences of the United States of America - 20 Sept 2022

Sekiyama Naotaka, Takaba Kiyofumi, Maki-Yonekura Saori, Akagi Ken-Ichi, Ohtani Yasuko, Imamura Kayo, Terakawa Tsuyoshi, Yamashita Keitaro, Inaoka Daigo, Yonekura Koji, Kodama Takashi S, Tochio Hidehito

Abstract excerpt

T cell intracellular antigen-1 (TIA-1) plays a central role in stress granule (SG) formation by self-assembly via the prion-like domain (PLD). In the TIA-1 PLD, amino acid mutations associated with neurodegenerative diseases, such as amyotrophic lateral sclerosis (ALS) or Welander distal myopathy (WDM), have been identified. However, how these mutations affect PLD self-assembly properties has remained elusive. In...

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Identifiers

PMID: 36112647
DOI: 10.1073/pnas.2122523119
PMCID: PMC9499527

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