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From TDP-43/RNA complex formation to disease-linked TDP-43 aggregation through a structural and cellular approach.

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Area of Science:

  • Neurobiology
  • Molecular Biology
  • Biochemistry

Background:

  • RNA-binding proteins (RBPs) are implicated in neurodegenerative diseases, often forming cytoplasmic inclusions.
  • TDP-43, an RBP, is frequently found in these inclusions, suggesting unique aggregation properties.

Purpose of the Study:

  • To investigate the mechanisms underlying TDP-43 aggregation.
  • To analyze the role of the N-terminal domain (NTD) of TDP-43 in its interactions and aggregation.

Main Methods:

  • In-depth structural analysis of the TDP-43 N-terminal domain (NTD).
  • Examination of TDP-43 binding cooperativity along GU-rich intronic sequences.

Main Results:

  • TDP-43 cooperativity on long GU-rich sequences antagonizes adjacent NTD/NTD interactions.
  • Cooperative binding facilitates NTD/NTD interactions between distinct GU-rich sequences, aiding intron compaction.
  • Discontinuous binding leads to aberrant adjacent interactions, promoting TDP-43 aggregation under stress.

Conclusions:

  • Physiological TDP-43 assembly on introns involves specific NTD/NTD interactions facilitated by cooperativity.
  • A lack of cooperativity disrupts normal interactions, leading to aberrant aggregation of TDP-43 RNA Recognition Motifs (RRMs).
  • These findings highlight specific vulnerabilities in TDP-43's structure and RNA binding that predispose it to aggregation compared to other RBPs.