Mechanisms tailoring the expression of heat shock proteins to proteostasis challenges

• Published in: The Journal of biological chemistry 2022-05, Vol.298 (5), p.101796-101796, Article 101796
• Main Authors: Alagar Boopathy, Lokha R., Jacob-Tomas, Suleima, Alecki, Célia, Vera, Maria
• Format: Article
• Language: English
• Subjects: acclimation; gene expression; heat shock factor 1; heat shock proteins; heat shock response; Heat-Shock Proteins - metabolism; Heat-Shock Response - physiology; JBC Reviews; Molecular Chaperones - genetics; Molecular Chaperones - metabolism; mRNA decay; Proteostasis; Signal Transduction; stress-regulated translation
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/j.jbc.2022.101796

All cells possess an internal stress response to cope with environmental and pathophysiological challenges. Upon stress, cells reprogram their molecular functions to activate a survival mechanism known as the heat shock response, which mediates the rapid induction of molecular chaperones such as the heat shock proteins (HSPs). This potent production overcomes the general suppression of gene expression and results in high levels of HSPs to subsequently refold or degrade misfolded proteins. Once the damage or stress is repaired or removed, cells terminate the production of HSPs and resume regular functions. Thus, fulfillment of the stress response requires swift and robust coordination between stress response activation and completion that is determined by the status of the cell. In recent years, single-cell fluorescence microscopy techniques have begun to be used in unravelling HSP-gene expression pathways, from DNA transcription to mRNA degradation. In this review, we will address the molecular mechanisms in different organisms and cell types that coordinate the expression of HSPs with signaling networks that act to reprogram gene transcription, mRNA translation, and decay and ensure protein quality control.