Fig. 1.

When the native states of proteins (N) become unstable under heat stress, sSHPs passively protect cells against potentially deleterious aggregates by remodeling their oligomeric landscapes. Both increased dissociation of dimeric subunits and a shift to higher oligomeric structures are accompanied by higher affinity for unfolded client molecules (U). The resulting hetero-oligomeric sSHP:client complexes agglomerate into an array of coaggregates that can be recovered by disaggregating Hsp100/Hsp70 chaperone teams.