The unfolded protein response (UPR) is an adaptive response to the stress that is caused by an accumulation of misfolded proteins in the lumen of the endoplasmic reticulum (ER). It is an important component of cellular homeostasis. During ER stress, the UPR increases the protein-folding capacity of the endoplasmic reticulum to relieve the stress. Failure to recover leads to apoptosis. Specific cellular mechanisms are required for the cellular recovery phase after UPR activation. Using bioinformatics tools, we identified a number of microRNAs that are predicted to decrease the mRNA expression levels for a number of critical components of the UPR. In this review, we discuss the potential role of microRNAs as key regulators of this pathway and describe how microRNAs may play an essential role in turning off the UPR after the stress has subsided.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3877167 | PMC |
| http://dx.doi.org/10.2478/s11658-013-0106-z | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Squamocin Suppresses Tumor Growth through Triggering an Endoplasmic Reticulum Stress-Associated Degradation of EZH2/MYC Axis.
Adv Sci (Weinh)
January 2025
School of Laboratory Medicine and Biotechnology, Southern Medical University, Guangzhou, 510515, China.
Despite substantial advances in the antitumor effects of annonaceous acetogenins (ACGs), the absence of a defined biological action mechanism remains a major barrier to their clinical application. Here, it is found that squamocin effectively depletes both EZH2 and MYC in multiple cancer cell lines, including head and neck squamous cell carcinoma, and gastric and colorectal cancer, demonstrating potent efficacy in suppressing these in vivo tumor models. Through the combination of surface plasmon resonance (SPR), differential scanning fluorimetry (DSF), and cellular thermal shift assay (CETSA), heat shock protein 90α (HSP90α) is identified as the direct binding target of squamocin.
View Article and Find Full Text PDFUnfolded protein response: An essential element of intestinal homeostasis and a potential therapeutic target for inflammatory bowel disease.
Acta Physiol (Oxf)
February 2025
Department of Medicine and Ageing Sciences, "G. d'Annunzio" University of Chieti-Pescara, Chieti, Italy.
Different physiological and pathological situations can produce alterations in the cell's endoplasmic reticulum (ER), leading to a condition known as ER stress, which can trigger an intricate intracellular signal transduction system known as the unfolded protein response (UPR). UPR is primarily tailored to restore proteostasis and ER equilibrium; otherwise, if ER stress persists, it can cause programmed cell death as a cytoprotective mechanism and drive inflammatory processes. Therefore, since intestinal cells strongly rely on UPR for their biological functions and unbalanced UPR has been linked to inflammatory, metabolic, and immune disorders, here we discussed the role of the UPR within the intestinal tract, focusing on the UPR contribution to inflammatory bowel disease development.
View Article and Find Full Text PDFFAM136A depletion induces mitochondrial stress and reduces mitochondrial membrane potential and ATP production.
FEBS Open Bio
January 2025
Department of Medical Technology, Faculty of Health Sciences, Kumamoto Health Science University, Kumamoto, Japan.
FAM136A deficiency has been associated with Ménière's disease. However, the underlying mechanism of action of this protein remains unclear. We hypothesized that FAM136A functions in maintaining mitochondria, even in HepG2 cells.
View Article and Find Full Text PDFMale sex determination maintains proteostasis and extends lifespan of daf-18/PTEN deficient C. elegans.
EMBO Rep
January 2025
The Zhongzhou Laboratory for Integrative Biology, Henan University, 450000, Zhengzhou, Henan, China.
Although females typically have a survival advantage, those with PTEN functional abnormalities face a higher risk of developing tumors than males. However, the differences in how each sex responds to PTEN dysfunction have rarely been studied. We use Caenorhabditis elegans to investigate how male and hermaphrodite worms respond to dysfunction of the PTEN homolog daf-18.
View Article and Find Full Text PDFIRE1 is a Promising Therapeutic Target in Pancreatic Cancer.
Am J Physiol Cell Physiol
January 2025
Department of General, Visceral, and Transplantation Surgery, University Hospital Heidelberg, Heidelberg, Germany.
Pancreatic cancer (PC) is one of the most aggressive malignancies, characterized by an increasing incidence and unfavorable prognosis. Despite recent advances, surgical resection combined with chemotherapy remains the only potentially curative therapeutic option. Therefore, it is of paramount importance to identify novel therapeutic targets and develop effective treatment strategies.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!