Nirbhik Acharya

1 Introduction Proteins carry out the vast majority of cellular functions. For well-folded proteins, the structure-function relationship is well established; sequence encodes structure and structure dictates function. Intrinsically disordered protein regions (IDRs), by contrast, lack a stable tertiary structure and instead exist as an ensemble of rapidly converting conformations [1].

Abstract Ubiquitin-binding shuttle proteins are important components of stress-induced biomolecular condensates in cells. Yeast Dsk2 scaffolds proteasome-containing condensates via multivalent interactions with proteasomes and ubiquitinated substrates under azide-induced mitochondrial stress or extended growth conditions. However, the molecular mechanisms underlying how these shuttle proteins work are unknown.