ArticleMolecular and cellular biology2013
Hyperthermia stress activates heat shock protein expression via propyl isomerase 1 regulation with heat shock factor 1.
Article in Molecular and cellular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.
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Who cites it
21 citing papers in PubMed, 1 synthesis or guideline pooled it, 46 citations in OpenAlex.
- Cancer therapy with iron oxide nanoparticles: Agents of thermal and immune therapies.Advanced drug delivery reviews · 2020Pooled it
- Magnetic hyperthermia in oncology: Nanomaterials-driven combinatorial strategies for synergistic therapeutic gains.Materials today. Bio · 2025Review
- Magnetic hyperthermia therapy enhances the chemoradiosensitivity of glioblastoma.Scientific reports · 2025Article
- Hyperthermia Potentiates the Effectiveness of Anticancer Drugs-Cisplatin and Tamoxifen on Ovarian Cancer Cells In Vitro.International journal of molecular sciences · 2024Article
- Magnetic Hyperthermia in Glioblastoma Multiforme Treatment.International journal of molecular sciences · 2024Review
- Pin1-catalyzed conformational regulation after phosphorylation: A distinct checkpoint in cell signaling and drug discovery.Science signaling · 2024Review
- Advances in screening hyperthermic nanomedicines in 3D tumor models.Nanoscale horizons · 2024Review
- Genetic inactivation of essentialMolecular biology of the cell · 2023Article
- Small Heat Shock Proteins Collaborate with FAIM to Prevent Accumulation of Misfolded Protein Aggregates.International journal of molecular sciences · 2022Article
- Roles of peptidyl-prolyl isomerase Pin1 in disease pathogenesis.Theranostics · 2021Review
- FAIM Is a Non-redundant Defender of Cellular Viability in the Face of Heat and Oxidative Stress and Interferes With Accumulation of Stress-Induced Protein Aggregates.Frontiers in molecular biosciences · 2020Article
- Enhancing the abscopal effect of radiation and immune checkpoint inhibitor therapies with magnetic nanoparticle hyperthermia in a model of metastatic breast cancer.International journal of hyperthermia : the official journal of European Society for Hyperthermic Oncology, North American Hyperthermia Group · 2019Article
- Optical Detection of Denatured Ferritin Protein via Plasmonic Gold Nanoparticles Exposure through Aminosilane Solution.Nanomaterials (Basel, Switzerland) · 2019Article
- SG formation relies on eIF4GI-G3BP interaction which is targeted by picornavirus stress antagonists.Cell discovery · 2019Article
- Magnetic hyperthermia therapy for the treatment of glioblastoma: a review of the therapy's history, efficacy and application in humans.International journal of hyperthermia : the official journal of European Society for Hyperthermic Oncology, North American Hyperthermia Group · 2018Review
- Natural Products to Fight Cancer: A Focus onToxins · 2018Review
- Nanoparticle-based hyperthermia distinctly impacts production of ROS, expression of Ki-67, TOP2A, and TPX2, and induction of apoptosis in pancreatic cancer.International journal of nanomedicine · 2017Article
- When Cancer Fights Back: Multiple Myeloma, Proteasome Inhibition, and the Heat-Shock Response.Molecular cancer research : MCR · 2015Review
- Landscape of Pin1 in the cell cycle.Experimental biology and medicine (Maywood, N.J.) · 2015Review
- Regulation of inflammatory transcription factors by heat shock protein 70 in primary cultured astrocytes exposed to oxygen-glucose deprivation.Neuroscience · 2015Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat shock proteins (HSPs), which are members of the chaperone family of proteins, are essential factors for cellular responses to environmental stressors, such as hyperthermia, and are antiapoptotic. The transcription of HSPs is mainly controlled by heat shock transcription factor 1 (HSF1). In response to environmental stress, HSF1 forms a trimer, undergoes hyperphosphorylation, and is translocated to the nucleus. In this study, we show that upon heat shock treatment of cells, a WW domain-containing propyl-isomerase, PIN1, is able to colocalize to and associate with phospho-HSF1 at Ser(326) in the nucleus via its WW domain. This interaction is required for the DNA-binding activity of HSF1 and is consistent with the lower induction of HSPs in PIN1-deficient cells. This function of PIN1 is further demonstrated by in vivo refolding and survival assays, which have shown that PIN1-deficient cells are temperature sensitive and develop apoptosis upon exposure to an environmental challenge. Moreover, the reduced levels of HSPs in PIN1-deficient cells resulted in less efficient refolding of denatured proteins. Based on our results, we propose a novel role for PIN1 whereby it acts as a stress sensor regulating HSF1 activity in response to stress on multiple levels through the transcriptional activation of stress response elements in embryonic fibroblast cells, tumor cells, and neurons.
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