Hsp70 chaperone provides Hsp104 with high efficiency in disaggregation and specificity towards aggregated substrates at the, otherwise limiting, cellular concentrations of adenine nucleotides.

The emergence of complementary electrostatic potentials after the prokaryotic-to-eukaryotic split drives physical and functional cooperation between canonical class A and class B J-proteins to boost protein disaggregation.

Recovery of proteins from aggregates by Hsp70 is boosted by the Hsp110 co-chaperone, which promotes abundant Hsp70 recruitment to aggregates and supports initial aggregate remodelling into small assemblies.

The bacterial AAA+ chaperone ClpL recognizes aggregated proteins via multiple contacts of its unique N-terminal domain and refolds them with high efficiency providing superior heat resistance.

A comparison in yeast and human cells reveals a remarkable variability in the properties of RNP granules and highlights a key role for protein disaggregation machines in regulating RNP granule assembly.

Overcoming image-processing problems in the analysis of the ClpB chaperone provides a new structural model and regulatory mechanism, based on clear density for the coiled-coil domain and supported by various biochemical data.

Skd3 (human ClpB) is a potent ATP-dependent mitochondrial protein disaggregase that is activated by the rhomboid protease, PARL, and inactivated by MGCA7-linked mutations.

The cisternae of the Golgi contain two functionally distinct domains: the central areas, which remain stationary, and the edges or rims, which are mobile.

Protein disaggregases employ two mechanically-linked ATPase rings that are under steric control by a wrapped-around coiled-coil belt.

Development of sequential mixing, single turnover stopped-flow approach reveals processive protein unfolding catalyzed by Escherichia coli ClpB.