ArticleCell death and differentiation2006
Coupling endoplasmic reticulum stress to the cell-death program: a novel HSP90-independent role for the small chaperone protein p23.
Article in Cell death and differentiation, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 73 citations in OpenAlex.
- Review
- Developmentally-regulated post-apocrine cell death ofFrontiers in cell and developmental biology · 2026Article
- Peroxisome proliferator-activated receptor gamma preserves intracellular homeostasis of insulin-resistant periodontal ligament stem cells.Annals of translational medicine · 2022Article
- The role of P53 up-regulated modulator of apoptosis (PUMA) in ovarian development, cardiovascular and neurodegenerative diseases.Apoptosis : an international journal on programmed cell death · 2021Review
- Echinacoside Upregulates Sirt1 to Suppress Endoplasmic Reticulum Stress and Inhibit Extracellular Matrix DegradationOxidative medicine and cellular longevity · 2021Article
- Overexpression of family with sequence similarity 134, member B (FAM134B) in colon cancers and its tumor suppressive properties in vitro.Cancer biology & therapy · 2020Article
- Mechanism of Apoptosis Induced by Curcumin in Colorectal Cancer.International journal of molecular sciences · 2019Review
- Curcumin Inhibits the PERK-eIF2Oxidative medicine and cellular longevity · 2019Article
- Dickkopf1 destabilizes atherosclerotic plaques and promotes plaque formation by inducing apoptosis of endothelial cells through activation of ER stress.Cell death & disease · 2017Article
- Article
- Imbalances in the Hsp90 Chaperone Machinery: Implications for Tauopathies.Frontiers in neuroscience · 2017Review
- Identification of RNA-binding Proteins in Macrophages by Interactome Capture.Molecular & cellular proteomics : MCP · 2016Article
- Endoplasmic reticulum stress and cancer.Journal of cancer prevention · 2014Review
- Gedunin inactivates the co-chaperone p23 protein causing cancer cell death by apoptosis.The Journal of biological chemistry · 2013Article
- Oxidative inhibition of Hsp90 disrupts the super-chaperone complex and attenuates pancreatic adenocarcinoma in vitro and in vivo.International journal of cancer · 2013Article
- The small co-chaperone p23 overexpressing transgenic mouse.Journal of neuroscience methods · 2013Article
- Role of the HSP90-associated cochaperone p23 in enhancing activity of the androgen receptor and significance for prostate cancer.Molecular endocrinology (Baltimore, Md.) · 2012Article
- The small chaperone protein p23 and its cleaved product p19 in cellular stress.Journal of molecular neuroscience : MN · 2012Article
- Mechanisms of Resistance to Hsp90 Inhibitor Drugs: A Complex Mosaic Emerges.Pharmaceuticals (Basel, Switzerland) · 2011Review
- Valosin-containing protein gene mutations: cellular phenotypes relevant to neurodegeneration.Journal of molecular neuroscience : MN · 2011Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The endoplasmic reticulum (ER) is the principal organelle for the biosynthesis of proteins, steroids and many lipids, and is highly sensitive to alterations in its environment. Perturbation of Ca(2+) homeostasis, elevated secretory protein synthesis, deprivation of glucose or other sugars, altered glycosylation and/or the accumulation of misfolded proteins may all result in ER stress, and prolonged ER stress triggers cell death. Studies from multiple laboratories have identified the roles of several ER stress-induced cell-death modulators and effectors through the use of biochemical, pharmacological and genetic tools. In the present work, we describe the role of p23, a small chaperone protein, in preventing ER stress-induced cell death. p23 is a highly conserved chaperone protein that modulates HSP90 activity and is also a component of the steroid receptors. p23 is cleaved during ER stress-induced cell death; this cleavage, which occurs close to the carboxy-terminus, requires caspase-3 and/or caspase-7, but not caspase-8. Blockage of the caspase cleavage site of p23 was associated with decreased cell death induced by ER stress. Immunodepletion of p23 or inhibition of p23 expression by siRNA resulted in enhancement of ER stress-induced cell death. While p23 co-immunoprecipitated with the BH3-only protein PUMA (p53-upregulated modulator of apoptosis) in untreated cells, prolonged ER stress disrupted this interaction. The results define a protective role for p23, and provide further support for a model in which ER stress is coupled to the mitochondrial intrinsic apoptotic pathway through the activities of BH3 family proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.