Redox-mediated regulation of low complexity domain self-association

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-beta 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-beta interactions that specify biologically relevant redox sensors.

Automated summary

Eukaryotic cells express protein domains with low sequence complexity that can undergo phase transition to form liquid-like droplets or hydrogels. These domains form cross-beta interactions through self-associative interactions and serve as biologically relevant redox sensors.