The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
HSF1: Guardian of Proteostasis in Cancer
Open accessAbstract
Proteomic instability is causally related to human diseases. In guarding proteome stability, the heat shock factor 1 (HSF1)-mediated proteotoxic stress response plays a pivotal role. Contrasting with its beneficial role of enhancing cell survival, recent findings have revealed a compelling pro-oncogenic role for HSF1. However, the mechanisms underlying the persistent activation and function of HSF1 within malignancy remain poorly understood. Emerging evidence reveals that oncogenic signaling mobilizes HSF1 and that cancer cells rely on HSF1 to avert proteomic instability and repress tumor-suppressive amyloidogenesis. In aggregate, these new developments suggest that cancer cells endure chronic proteotoxic stress and that proteomic instability is intrinsically associated with malignant state, a characteristic that could be exploited to combat cancer.
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Cites
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AMPK Phosphorylation of Raptor Mediates a Metabolic Checkpoint
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“Given that elevated lipogenesis is widespread in human cancers and critical to membrane synthesis necessary for rapid cancer cell proliferation [86], this lipogenic effect of HSF1 is proposed to promote development of hepatocellular carcinomas [62].”
BackgroundThe AMPK signalling pathway coordinates cell growth, autophagy and metabolism
Mihaylova, M. M., & Shaw, R. J. (2011) · Nature Cell Biology · doi:10.1038/ncb2329 · Cited by 2,923
The Biology of Proteostasis in Aging and Disease
Labbadia, J., & Morimoto, R. I. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-033955 · Cited by 1,472
Targeting RAS–ERK signalling in cancer: promises and challenges
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AMPK: positive and negative regulation, and its role in whole-body energy homeostasis
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The Reprogramming of Tumor Stroma by HSF1 Is a Potent Enabler of Malignancy
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Cited by
Regulation of heat shock transcription factors and their roles in physiology and disease
Gomez-Pastor, R., Burchfiel, E. T., & Thiele, D. J. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.73 · Cited by 849
Alcohol-abuse drug disulfiram targets cancer via p97 segregase adaptor NPL4
Skrott, Z., Mistrik, M., Andersen, K. K., Friis, S., Majera, D., Gursky, J., Ozdian, T., Bartkova, J., Turi, Z., Moudry, P., et al. (2017) · Nature · doi:10.1038/nature25016 · Cited by 807
The Biology of Aging and Cancer: A Brief Overview of Shared and Divergent Molecular Hallmarks
Aunan, J. R., Cho, W. C., & Søreide, K. (2017) · Aging and disease · doi:10.14336/ad.2017.0103 · Cited by 373
Signaling pathways in cancer‐associated fibroblasts: recent advances and future perspectives
Fang, Z., Meng, Q., Xu, J., Wang, W., Zhang, B., Liu, J., Liang, C., Hua, J., Zhao, Y., Yu, X., et al. (2023) · Cancer Communications · doi:10.1002/cac2.12392 · Cited by 280
Ferrari, N., Ranftl, R., Chicherova, I., Slaven, N. D., Moeendarbary, E., Farrugia, A. J., Lam, M., Semiannikova, M., Westergaard, M. C. W., Tchou, J., et al. (2019) · Nature Communications · doi:10.1038/s41467-018-07987-0 · Cited by 164
Metadata
- Authors
- Dai, C., & Sampson, S. B.
- Venue
- Trends in Cell Biology
- Publisher
- Elsevier BV
- Published
- 2016-01
- Volume
- 26
- Issue
- 1
- Pages
- 17-28
- ISSN
- 0962-8924 (ISSN-L)
- OpenAlex
- W2213407375
- Cited by
- 210
- References
- 9
- FWCI
- 1.20
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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