HSF1: A Protein Regulating Heat Shock and Cellular Processes (G3297)

Target Name: HSF1

NCBI ID: G3297

HSF1

HSF1: A Protein Regulating Heat Shock and Cellular Processes

Heat shock transcription factor 1 (HSF1) is a protein that plays a crucial role in the regulation of gene expression in response to thermal stress, such as heat shock. It is a key transcription factor that is activated in response to temperature increase and can induce a range of cellular responses, including the expression of heat shock-responsive genes.

HSF1 is a 22-kDa protein that is expressed in a variety of tissues, including muscle, heart, and brain. It is highly conserved across different species, and its function has been extensively studied.

One of the key functions of HSF1 is to regulate the expression of heat shock-responsive genes. These genes are encoding proteins that are involved in various cellular processes, including stress response, DNA damage repair, and metabolism. By regulating the expression of these genes, HSF1 allows cells to respond to thermal stress and maintain cellular homeostasis.

HSF1 can also play a role in the regulation of cell cycle progression. It has been shown to play a role in the regulation of G1 cell cycle progression to S-phase, which is a critical step in the cell cycle that allows for the expression of genetic Maintenance programs.

HSF1 has also been shown to play a role in the regulation of angiogenesis, the process by which new blood vessels are formed. It has been shown to regulate the expression of genes involved in blood vessel formation and maintenance, such as PLC/PKG-associated genes, which are involved in the regulation of ion and water transport.

In addition to its role in gene regulation, HSF1 has also been shown to play a role in cellular signaling. It has been shown to play a role in the regulation of TGF-β signaling, which is a complex signaling pathway involved in the regulation of cellular growth, differentiation, and inflammation.

Given its widespread expression and its critical role in cellular processes, HSF1 is a promising drug target. Researchers have identified several potential small molecules that can inhibit HSF1 activity, and these molecules have been shown to have a variety of therapeutic effects, including the inhibition of cancer growth and the regulation of cellular aging.

In addition to its potential therapeutic applications, HSF1 is also of interest as a biomarker for various diseases, including cancer, neurodegenerative diseases, and cardiovascular disease. The expression of HSF1 has been shown to be altered in a variety of disease states, including cancer, neurodegenerative diseases, and cardiovascular disease.

Furthermore, the regulation of HSF1 by temperature is a powerful insight into the complex mechanisms of thermal stress and its impact on the cell. The study of HSF1 has the potential to provide new insights into the regulation of cellular processes and the development of new therapeutic approaches for a variety of diseases.

In conclusion, HSF1 is a protein that plays a critical role in the regulation of gene expression in response to thermal stress. Its function is the regulation of heat shock-responsive genes, the regulation of cell cycle progression, the regulation of angiogenesis and the regulation of cellular signaling. It is a potential drug target and a biomarker for various diseases. Further research is needed to fully understand the mechanisms of HSF1 regulation and its potential therapeutic applications.

Protein Name: Heat Shock Transcription Factor 1

Functions: Functions as a stress-inducible and DNA-binding transcription factor that plays a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones, heat shock proteins (HSPs), that protect cells from cellular insult damage (PubMed:1871105, PubMed:11447121, PubMed:1986252, PubMed:7760831, PubMed:7623826, PubMed:8946918, PubMed:8940068, PubMed:9341107, PubMed:9121459, PubMed:9727490, PubMed:9499401, PubMed:9535852, PubMed:12659875, PubMed:12917326, PubMed:15016915, PubMed:25963659, PubMed:26754925, PubMed:18451878). In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form (PubMed:9727490, PubMed:11583998, PubMed:16278218). Upon exposure to heat and other stress stimuli, undergoes homotrimerization and activates HSP gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of HSP genes (PubMed:1871105, PubMed:1986252, PubMed:8455624, PubMed:7935471, PubMed:7623826, PubMed:8940068, PubMed:9727490, PubMed:9499401, PubMed:10359787, PubMed:11583998, PubMed:12659875, PubMed:16278218, PubMed:25963659, PubMed:26754925). Upon heat shock stress, forms a chromatin-associated complex with TTC5/STRAP and p300/EP300 to stimulate HSR transcription, therefore increasing cell survival (PubMed:18451878). Activation is reversible, and during the attenuation and recovery phase period of the HSR, returns to its unactivated form (PubMed:11583998, PubMed:16278218). Binds to inverted 5'-NGAAN-3' pentamer DNA sequences (PubMed:1986252, PubMed:26727489). Binds to chromatin at heat shock gene promoters (PubMed:25963659). Activates transcription of transcription factor FOXR1 which in turn activates transcription of the heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH-dependent reductase DHRS2 (PubMed:34723967). Also serves several other functions independently of its transcriptional activity. Involved in the repression of Ras-induced transcriptional activation of the c-fos gene in heat-stressed cells (PubMed:9341107). Positively regulates pre-mRNA 3'-end processing and polyadenylation of HSP70 mRNA upon heat-stressed cells in a symplekin (SYMPK)-dependent manner (PubMed:14707147). Plays a role in nuclear export of stress-induced HSP70 mRNA (PubMed:17897941). Plays a role in the regulation of mitotic progression (PubMed:18794143). Also plays a role as a negative regulator of non-homologous end joining (NHEJ) repair activity in a DNA damage-dependent manner (PubMed:26359349). Involved in stress-induced cancer cell proliferation in a IER5-dependent manner (PubMed:26754925)

The "HSF1 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about HSF1 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
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•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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