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Pessa, J. C., Joutsen, J., & Sistonen, L. Transcriptional reprogramming at the intersection of the heat shock response and proteostasis. Molecular cell. Added by: Dr. Enrique Feoli (21/08/2025, 16:45) Last edited by: Dr. Enrique Feoli (21/08/2025, 17:11) |
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| Resource type: Journal Article ID no. (ISBN etc.): 1097-4164 BibTeX citation key: Pessa View all bibliographic details  |
Categories: BioAcyl Corp Subcategories: Integrated stress response Keywords: chromatin, enhancer, heat shock factor, heat shock response, HSF, HSR, Pol II, post-translational modification, proteostasis, PTM, RNA polymerase II, transcription, transcription factor Creators: Joutsen, Pessa, Sistonen Collection: Molecular cell |
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| Abstract |
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Cellular homeostasis is constantly challenged by a myriad of extrinsic and intrinsic stressors. To mitigate the stress-induced damage, cells activate transient survival programs. The heat shock response (HSR) is an evolutionarily well-conserved survival program that is activated in response to proteotoxic stress. The HSR encompasses a dual regulation of transcription, characterized by rapid activation of genes encoding molecular chaperones and concomitant global attenuation of non-chaperone genes. Recent genome-wide approaches have delineated the molecular depth of stress-induced transcriptional reprogramming. The dramatic rewiring of gene and enhancer networks is driven by key transcription factors, including heat shock factors (HSFs), that together with chromatin-modifying enzymes remodel the 3D chromatin architecture, determining the selection of either gene activation or repression. Here, we highlight the current advancements of molecular mechanisms driving transcriptional reprogramming during acute heat stress. We also discuss the emerging implications of HSF-mediated stress signaling in the context of physiological and pathological conditions.
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| Notes |
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Heat shock factor-mediated stress signaling in physiology and pathology
(A) HSFs mediate stress signaling in a broad selection of physiological processes.
(B) Chronic stress signaling leads to dysregulation of HSF-mediated signaling. The effects of dysregulated HSFs have been primarily investigated in cancer and neurodegenerative diseases. High levels of HSF1 correlate with malignant transformation, while the function of HSF2 in tumorigenesis is context dependent. Cooperation of HSF1 and HSF2 can also promote disease progression in specific cancer types. In contrast, HSF-dependent collapse of proteostasis is evident in many neurodegenerative diseases. The function and stoichiometry of HSF1-HSF2 heterotrimers in pathology remain poorly understood.
Added by: Dr. Enrique Feoli Last edited by: Dr. Enrique Feoli |
