Model depicting the roles of Hsp42 and Hsp26 in aggregate sorting in yeast cells experiencing sublethal folding stress. Hsp42 exclusively associates with peripheral protein aggregates during physiological folding stress (37°C) but is absent from juxtanuclear aggregates (JUNQ). The formation of peripheral foci depends on the elongated NTD of Hsp42. Hsp26 is absent from protein aggregates at 37°C but associates with peripheral and juxtanuclear aggregates during lethal heat stress (45°C). Hsp42 does not associate with the IPOD compartment harboring amyloidogenic proteins close to the vacuole. Ubiquitination (Ub) might serve as a sorting signal for juxtanuclear aggregates.