Viruses, endoplasmic reticulum stress, and interferon responses.
Reads0
Chats0
TLDR
Emerging evidence suggests that viruses not only interfere with the interferon system involving PKR but also manipulate the programs emanating from the ER in a complex way, which may facilitate viral replication or pathogenesis.Abstract:
Viral infection induces endoplasmic reticulum (ER) stress and interferon responses. While viral double-stranded RNA intermediates trigger interferon responses, viral polypeptides synthesized during infection stimulate ER stress. Among the interferon-regulated gene products, the double-stranded RNA-dependent protein kinase (PKR) plays a key role in limiting viral replication. Thus, to establish productive infection, viruses have evolved mechanisms to overcome the deleterious effects of PKR. It has become clear that ER stress causes translational attenuation and transcriptional upregulation of genes encoding proteins that facilitate folding or degradation of proteins. Notably, prolonged ER stress triggers apoptosis. Therefore, viruses are confronted with the consequences of ER stress. Emerging evidence suggests that viruses not only interfere with the interferon system involving PKR but also manipulate the programs emanating from the ER in a complex way, which may facilitate viral replication or pathogenesis. This review highlights recent progress in these areas.read more
Citations
More filters
Journal ArticleDOI
ER stress-induced cell death mechanisms
Renata Sano,John C. Reed +1 more
TL;DR: Recent advances in understanding the diversity of molecular mechanisms that govern ER stress signaling in health and disease are summarized.
Journal ArticleDOI
A molecular web: endoplasmic reticulum stress, inflammation, and oxidative stress.
Namrata Chaudhari,Priti Talwar,Avinash Parimisetty,Christian Lefebvre d'Hellencourt,Palaniyandi Ravanan +4 more
TL;DR: The UPR signaling pathways, and networking between ER stress-induced inflammatory pathways, oxidative stress, and mitochondrial signaling events, which further induce or exacerbate ER stress are discussed.
Journal ArticleDOI
Endoplasmic reticulum stress in health and disease
Lihong Zhao,Susan L. Ackerman +1 more
TL;DR: Recent progress suggests that ER stress and UPR play key roles in the immune response, diabetes, tumor growth under hypoxic conditions, and in some neurodegenerative diseases.
Journal ArticleDOI
Mechanisms and consequences of macrophage apoptosis in atherosclerosis
Tracie A. Seimon,Ira Tabas +1 more
TL;DR: In this paper, the role of phagocytic clearance of apoptotic macrophages, a process known as efferocytosis, in the dichotomous roles of macrophage apoptosis in early vs. advanced lesions was examined.
Journal ArticleDOI
Endoplasmic Reticulum Stress: Its Role in Disease and Novel Prospects for Therapy
TL;DR: The cell reacts to ER stress by initiating a defensive process, called the unfolded protein response (UPR), which is comprised of cellular mechanisms aimed at adaptation and safeguarding cellular survival or, in cases of excessively severe stress, at initiation of apoptosis and elimination of the faulty cell.
References
More filters
Journal ArticleDOI
How cells respond to interferons
TL;DR: The Janus kinases and signal transducers and activators of transcription, and many of the interferon-induced proteins, play important alternative roles in cells, raising interesting questions as to how the responses to the interFERons intersect with more general aspects of cellular physiology and how the specificity of cytokine responses is maintained.
Journal ArticleDOI
XBP1 mRNA Is Induced by ATF6 and Spliced by IRE1 in Response to ER Stress to Produce a Highly Active Transcription Factor
TL;DR: The transcription factor XBP1, a target of ATF6, is identified as a mammalian substrate of such an unconventional mRNA splicing system and it is shown that only the spliced form of X BP1 can activate the UPR efficiently.
Journal ArticleDOI
Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta.
TL;DR: It is shown that caspase-12 is localized to the ER and activated by ER stress, including disruption of ER calcium homeostasis and accumulation of excess proteins in ER, but not by membrane- or mitochondrial-targeted apoptotic signals, which may contribute to amyloid-β neurotoxicity.
Journal ArticleDOI
Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1.
Fumihiko Urano,Xiaozhong Wang,Anne Bertolotti,Yuhong Zhang,Peter Chung,Heather P. Harding,David Ron +6 more
TL;DR: Malfolded proteins in the endoplasmic reticulum induce cellular stress and activate c-Jun amino-terminal kinases (JNKs or SAPKs), and Mammalian homologs of yeast IRE1, which activate chaperone genes in response to ER stress, also activated JNK, and I RE1alpha-/- fibroblasts were impaired in JNK activation by ER stress.
Journal ArticleDOI
Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
Anne Bertolotti,Yuhong Zhang,Linda M. Hendershot,Linda M. Hendershot,Heather P. Harding,David Ron +5 more
TL;DR: In this article, the lumenal domains of transmembrane protein kinases (PERK and IRE1) were found to be functionally interchangeable in mediating an ER stress response and that in unstressed cells, both L1 and L2 domains formed a stable complex with the ER chaperone BiP.
Related Papers (5)
XBP1 mRNA Is Induced by ATF6 and Spliced by IRE1 in Response to ER Stress to Produce a Highly Active Transcription Factor
Signal integration in the endoplasmic reticulum unfolded protein response
David Ron,Peter Walter +1 more