Heat shock induces relocalization of epigenetic modifiers to the nucleolus, which acts as a dedicated protein quality control center that is indispensable for recovery of epigenetic regulators and epigenetic modifications.

Multiple iso-energetic-specific interactions involving the intrinsically-disordered region of sHSP HSPB1 define a quasi-ordered state, providing insights into inherited disease-associated mutations within the region that are thought to be disordered.

Ribosome assembly is monitored to promote proteostatis through a system whereby unassembled ribosomal proteins lead to activation of heat shock factor 1 and inactivation of the RP gene activator Ifh1.

Small decreases in pH associated with cellular stress conditions unleash a cryptic mode of client binding in a ubiquitously expressed human small heat shock protein that is more effective at delaying client aggregation.

Hsp70 restricts DNA binding activity of Hsf1 to control the width and amplitude of the heat-shock regulon.

Integration of complementary computational approaches reveals an evolutionarily conserved interaction interface between molecular chaperones Hsp70 and Hsp40, rationalizing previous observations.

DynAPs reveal that biological phase separation provides the organizing principle for the complex process of dynein motor assembly in cells with motile cilia.

A new unfolded protein response has been discovered that is distinct from the heat shock response and protects mammalian cells from proteotoxic stress.

Head-to-head interactions of regulatory coiled-coil domains control activity of the central bacterial AAA+ protein ClpC by promoting formation of a reversible resting state.

Transcriptomics is shedding new light on the relationship between photosynthetic algae and salamander eggs.