Hsf-1 and POB1 induce drug sensitivity and apoptosis by inhibiting Ralbp1
Open accessAbstract
Hsf-1 (heat shock factor-1) is a transcription factor that is known to regulate cellular heat shock response through its binding with the multispecific transporter protein, Ralbp1. Results of present studies demonstrate that Hsf-1 causes specific and saturable inhibition of the transport activity of Ralbp1 and that the combination of Hsf-1 and POB1 causes nearly complete inhibition through specific bindings with Ralbp1. Augmentation of cellular levels of Hsf-1 and POB1 caused dramatic apoptosis in non-small cell lung cancer cell line H358 through Ralbp1 inhibition. These findings indicate a novel model for mutual regulation of Hsf-1 and Ralbp1 through Ralbp1-mediated sequestration of Hsf-1 in the cellular cytoskeleton and Hsf-1-mediated inhibition of the transport activity of membrane-bound Ralbp1.
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In the unstressed state, HSF1 and Rlip are mutually inhibitory, with HSF1 inhibiting Rlip efflux and Rlip sequestering HSF1 in the cytosol.
“In the unstressed state, HSF1 and Rlip are mutually inhibitory, with HSF1 inhibiting the efflux function of Rlip, and Rlip sequestering HSF1 in the cytosol.”
From Rlip76: An Unexplored Player in Neurodegeneration and Alzheimer’s Disease? (2022) · cites this paper as [38]
In “Hsf-1 and POB1 Inhibit Ralbp1” (page not provided), the paper reports that Hsf-1 inhibits Ralbp1 transport and describes an unstressed cytoplasmic complex containing both proteins. It proposes mutual inhibition, including Ralbp1 inhibition of Hsf-1 activity, as a model rather than establishing it as an unqualified fact. (LLM, conf=0.83)
Experimental — accuracy not yet measuredUnder stress, Rlip and HSF1 dissociate, freeing Rlip to catalyze ATP-dependent efflux of glutathione conjugates and xenobiotics and freeing HSF1 to translocate to the nucleus to activate stress response pathways.
“Under stress, Rlip and HSF1 dissociate [31,38], freeing Rlip to catalyze the ATP-dependent efflux of glutathione conjugates and xenobiotics and freeing HSF1 to translocate to the nucleus to activate stress response pathways [31,38].”
From Rlip76: An Unexplored Player in Neurodegeneration and Alzheimer’s Disease? (2022) · cites this paper as [38]
The introduction reports that stress releases Hsf-1 from its complex with Ralbp1, allowing Hsf-1 to enter the nucleus, and describes Ralbp1’s ATP-dependent efflux of xenobiotics and glutathione conjugates. It presents the further claim that stress-induced dissociation frees Ralbp1’s efflux activity as a model prediction, rather than an established consequence of stress. (LLM, conf=0.83)
Experimental — accuracy not yet measuredStress induces Rlip translocation to the nucleus, suggesting Rlip may have a role in transcriptional regulation.
“Interestingly, Singhal et al. reported that stress also induces Rlip translocation to the nucleus, suggesting that Rlip may also have a role in transcriptional regulation [38].”
From Rlip76: An Unexplored Player in Neurodegeneration and Alzheimer’s Disease? (2022) · cites this paper as [38]
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- [21]21. Sambrook, J., Fritsch, E. F., and Miniatis, T. (1989) Molecular Cloning: A Laboratory Manual , 2nd Ed., pp. 17.3-17.9, Cold Spring Harbor University, Cold Spring Harbor, NY
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Singhal, S. S., Figarola, J., Singhal, J., Leake, K., Nagaprashantha, L., Lincoln, C., Gabriel Gugiu, B., Horne, D., Jove, R., Awasthi, S., et al. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.08.020 · Cited by 20 · see citing works
Novel Compound 1, 3-bis (3, 5-dichlorophenyl) urea Inhibits Lung Cancer Progression
Singhal, S. S., Figarola, J., Singhal, J., Nagaprashantha, L., Berz, D., Rahbar, S., & Awasthi, S. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.09.022 · Cited by 14 · see citing works
Self-citationRlip76: An Unexplored Player in Neurodegeneration and Alzheimer’s Disease?
Hindle, A., Singh, S. P., Pradeepkiran, J. A., Bose, C., Vijayan, M., Kshirsagar, S., Sawant, N. A., & Reddy, P. H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116098 · Cited by 14 · see citing works
- Authors
- Singhal, S. S., Yadav, S., Drake, K., Singhal, J., & Awasthi, S.
- Affiliations
- University of North Texas Health Science Center (US)
- Corresponding author
- Awasthi, Sanjay
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2008-07
- Volume
- 283
- Issue
- 28
- Pages
- 19714-19729
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2443664
- OpenAlex
- W1996690569
- Cited by
- 55
- References
- 0
- Citations by year
- 2025: 1 · 2024: 2 · 2023: 1 · 2022: 3 · 2021: 2 · 2020: 2 · 2019: 3 · 2018: 1 · 2017: 3 · 2016: 2 · 2015: 3 · 2014: 4 · 2013: 6 · 2012: 2
- FWCI
- 2.53
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Public Health Service (ISIORR018999-01A1)
- National Cancer Institute (CA 77495, R01CA104661, R01CA077495, CA104661)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- HSF1, RALBP1, heat shock response, apoptosis, drug sensitivity, non-small cell lung cancer, H358 cells, transcription factor regulation
- MeSH terms
- Heat Shock Transcription Factors, Antineoplastic Agents, Biological Transport, Calcium-Binding Proteins, Carcinoma, Non-Small-Cell Lung, Cytoskeleton, DNA-Binding Proteins, Humans, Lung Neoplasms, Protein Binding, Transcription Factors, Apoptosis, ATP-Binding Cassette Transporters, Heat-Shock Response, Drug Resistance, Neoplasm, K562 Cells, GTPase-Activating Proteins, Intracellular Signaling Peptides and Proteins
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