Redox-mediated regulation of low complexity domain self-association

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7 Scopus citations


Eukaryotic cells express thousands of protein domains long believed to function in the absence of molecular order. These intrinsically disordered protein (IDP) domains are typified by gibberish-like repeats of only a limited number of amino acids that we refer to as domains of low sequence complexity. A decade ago, it was observed that these low complexity (LC) domains can undergo phase transition out of aqueous solution to form either liquid-like droplets or hydrogels. The self-associative interactions responsible for phase transition involve the formation of specific cross-β structures that are unusual in being labile to dissociation. Here we give evidence that the LC domains of two RNA binding proteins, ataxin-2 and TDP43, form cross-β interactions that specify biologically relevant redox sensors.

Original languageEnglish (US)
Pages (from-to)111-118
Number of pages8
JournalCurrent Opinion in Genetics and Development
StatePublished - Apr 2021

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology


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