ArticleThe EMBO journal1997
A pathway distinct from the mammalian unfolded protein response regulates expression of endoplasmic reticulum chaperones in non-stressed cells.
Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
28 citing papers in PubMed, 84 citations in OpenAlex.
- Imbalanced unfolded protein response signaling contributes to 1-deoxysphingolipid retinal toxicity.Nature communications · 2023Article
- Article
- Juvenile hormone differentially regulates twoThe Journal of biological chemistry · 2017Article
- Endoplasmic Reticulum Stress and Homeostasis in Reproductive Physiology and Pathology.International journal of molecular sciences · 2017Review
- PERK Is a Haploinsufficient Tumor Suppressor: Gene Dose Determines Tumor-Suppressive Versus Tumor Promoting Properties of PERK in Melanoma.PLoS genetics · 2016Article
- Review
- Mechanistic rationale for targeting the unfolded protein response in pre-B acute lymphoblastic leukemia.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- GRP78/BiP is a novel downstream target of IGF-1 receptor mediated signaling.Journal of cellular physiology · 2012Article
- GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum.Biochimica et biophysica acta · 2012Review
- Hepatic nuclear factor 1alpha (HNF1alpha) dysfunction down-regulates X-box-binding protein 1 (XBP1) and sensitizes beta-cells to endoplasmic reticulum stress.The Journal of biological chemistry · 2011Article
- Endoplasmic reticulum stress and the unfolded protein response in nonalcoholic fatty liver disease.Antioxidants & redox signaling · 2011Review
- Detecting and quantitating physiological endoplasmic reticulum stress.Methods in enzymology · 2011Article
- A Phos-tag-based approach reveals the extent of physiological endoplasmic reticulum stress.PloS one · 2010Article
- Plasma cell differentiation initiates a limited ER stress response by specifically suppressing the PERK-dependent branch of the unfolded protein response.Cell stress & chaperones · 2010Article
- Regulated increase in folding capacity prevents unfolded protein stress in the ER.Journal of cell science · 2010Article
- Trypanosoma brucei UDP-glucose:glycoprotein glucosyltransferase has unusual substrate specificity and protects the parasite from stress.Eukaryotic cell · 2009Article
- Dual function of pancreatic endoplasmic reticulum kinase in tumor cell growth arrest and survival.Cancer research · 2008Article
- Up-regulation of GRP78 and antiapoptotic signaling in murine peritoneal macrophages exposed to insulin.Journal of leukocyte biology · 2005Article
- NAD(P)H oxidase Nox-4 mediates 7-ketocholesterol-induced endoplasmic reticulum stress and apoptosis in human aortic smooth muscle cells.Molecular and cellular biology · 2004Article
- Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death.The Journal of cell biology · 2004Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The stress-induced unfolded protein response (UPR) is the only signaling pathway known to regulate expression of genes encoding the resident endoplasmic reticulum (ER) molecular chaperones and folding enzymes, yet these genes are constitutively expressed in all cells. We have examined the expression of ER chaperones in several cell lines that are dependent on a variety of cytokines for growth and survival. When the various cell lines were deprived of essential growth factors, mRNA levels of the ER chaperones BiP and GRP94 decreased dramatically. Re-stimulation of ligand-deprived cells with the appropriate growth factor induced BiP and GRP94 as delayed-early response genes. Cytokine induction of BiP and GRP94 biosynthesis was not preceded by a burst of glycoprotein traffic through the ER nor accompanied by expression of the CHOP transcription factor. The glycosylation inhibitor tunicamycin potently induced expression of both ER chaperones and CHOP in ligand-deprived cells, demonstrating that the UPR pathway remains functionally intact in the absence of growth factor-mediated signaling. Therefore, basal expression of ER chaperones is dependent upon and regulated by a mitogenic pathway distinct from the stress-inducible UPR cascade and this probably controls expression of ER chaperones and folding enzymes needed to assist protein biogenesis in the ER of normal, non-stressed cells.
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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.