Aberrant protein interactions in amyloid disease

  • Martin Vabulas R
  • Ulrich Hartl F
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How protein aggregation causes cytotoxicity and disease is not yet well understood. a recent study, employing artificial β-sheet proteins as a model, provided new insight into the mechanisms by which amyloid-like aggregation can cause far-reaching disturbances in the proteome network. Quantitative proteomics revealed that a group of metastable proteins are particularly vulnerable to sequestration by the aggregates. these proteins are generally large in size and enriched in unstructured regions, properties that are associated with a high degree of functionality as network hubs. they have key functions in transcription, translation, trafficking and cytoskeletal organization. thus, co-aggregation of a diverse set of proteins with essential functions is likely to explain, at least in part, the multi-factorial and severe toxicity resulting from intracellular amyloidogenesis.

Author-supplied keywords

  • Aggregate cytotoxicty
  • Aggregation
  • Amyloids
  • Protein folding
  • Proteomics

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  • R. Martin Vabulas

  • F. Ulrich Hartl

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