Summary
Cells often encounter stressful situations and respond to them with a stereotypical program to ensure survival. These responses involve increased expression of stress response factors, formation of stress granules (SGs), and shutting down of essential cellular processes, including RNA splicing, global translation, and nucleocytoplasmic transport. These adaptive changes are protective in the short term but need to be reversed once the stress has subsided so that cells can return to their normal activities. The molecular mechanisms involved in this reversal are only poorly understood. On pages 1409 and 1410 of this issue, Maxwell et al. (1) and Gwon et al. (2), respectively, reveal that recovery from heat stress requires tagging proteins with polyubiquitin chains. Together, these studies establish that ubiquitination has surprising regulatory and context-specific roles in the heat-stress response and emphasize that more attention should be paid to the stress recovery phase.