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Sustained PERK activation can amplify PERK signaling by further enhancing CNPY2 expression via direct transactivation through CHOP.
Our results indicate that tauopathy-associated PERK alleles are functional hypomorphs during the UPR. We propose that reduced PERK function leads to neurodegeneration by increasing neuronal vulnerability to ER stress-associated damage.
partial pancreatic endoplasmic reticulum kinase (PERK )inhibition induced ER chaperone BiP expression in islets, increased glucose-stimulated calcium transit and islet insulin contents and enhanced glucose-stimulated insulin secretion
A PERK-miR-211 axis suppresses circadian regulators and protein synthesis to promote cancer cell survival.
The protein but not the mRNA level of ORP150, a nucleotide exchange factor which can substitute for SIL1, was increased in the cerebellum of GSK2606414-treated woozy mice, suggesting that translational recovery promoted the synthesis of this alternative BiP co-factor
These findings uncover an entirely new biological link among PERK, neuronal intrinsic properties, aging, and cognitive function
CO-stimulated PERK activation and enhanced the levels of FGF21 via the eIF2alpha-ATF4 signaling pathway. The induction of FGF21 by CO attenuated endoreticulum stress- or diet-induced, obesity-dependent hepatic steatosis.
Leishmania infection results in phosphorylation and activation of host PERK enzyme and increased transcription of genes of inhibitor of apoptosis gene family (cIAP) mRNA.
These results suggest that the translational control mediated by PERK is a critical determinant of extracellular matrix secretion in chondrocytes.
PERK regulates oligodendrocyte survival during differentiation.
Data suggest the activation of PERK is part of a protective response to mutant rhodopsin that ultimately limits photoreceptor cell death.
Atg7 ablation mainly induced the PERK-ATF4-CHOP axis of the endoplasmic reticulum (ER) stress response in growth plate chondrocytes.
heme-regulated inhibitor (HRI), protein kinase R (PKR), PKR-like endoplasmic reticulum kinase, (PERK) and general control non-depressible 2 (GCN2) are sufficient for the integrated stress response; there are no additional eIF2alpha kinases in vertebrates
these findings reveal a new crucial combined effect of the silencing of PERK and ATF4 in modulating ER stressmediated apoptosis during chondrocyte differentiation and proliferation.
Activation of the ER stress execution proteins, PERK and CHOP10, was evaluated to determine whether this process was involved in 15d-PMJ2 cell death. 15d-PMJ2 increased the phosphorylation of PERK and expression of CHOP10 in tumorigenic but not nontumorigenic cells
In response to endoplasmic reticulum stress, activation of PERK coordinates the integrated stress response by phosphorylating eIF2alpha, which is then quickly dephosphorylated by the GADD34 complex. Data imply dual role of the ISR in promoting and inhibiting medulloblastoma tumorigenesis.
These findings identify DLK as a central regulator of not only JNK but also PERK stress signaling in neurons, with both pathways contributing to neurodegeneration.
PERK has a role in mediating the internal ribosome entry site-dependent translational activation of mRNAs encoding angiogenic growth factors after ischemic stress
NDRG2 is a novel ERS-responsive protein and acts as PERK co-factor to facilitate PERK branch, thereby contributing to ERS-induced apoptosis.
the impaired working memory in forebrain-specific Perk knockout mice may stem from altered Gq protein-coupled intracellular Ca(2+) dynamics in cortical pyramidal neurons.
The data also support a potential role for the PERK/eIF2a/ATF4 axis in modulating cell viability in irradiated glioblastoma multiforme (GBM). The dual function of PERK as a mediator of survival and death may be exploited to enhance the efficacy of radiation therapy
Under hypoxic conditions, activation of the PERK branch of the unfolded protein response can suppress the levels and activity of HIF1alpha by preventing efficient HIF1alpha translation. Activation of PERK inhibits de novo HIF1alpha protein synthesis by preventing the RNA-binding protein, YB-1, from interacting with the HIF1alpha mRNA 5'UTR.
Non-structural protein 2B of human rhinovirus16 induced an endoplasmic reticulum stress response through the PERK and ATF6 pathways rather than the IRE1 pathway.
Results show that PERK inhibition attenuates the abnormalities of the secretory pathway and the increased apoptotic rate induced by SIL1 knockdown in HeLa cells.
unfolded protein response mediated by the PERK pathway is causally related to the development of intervertebral disc degeneration.
partial pancreatic endoplasmic reticulum (ER) kinase (PERK)inhibition induced ER chaperone BiP expression in islets, increased glucose-stimulated calcium transit and islet insulin contents and enhanced glucose-stimulated insulin secretion
Coordination between two branches of the unfolded protein response determines apoptotic cell fate so that PERK attenuates IRE1 via RPAP2 to abort failed endoplasmic reticulum stress adaptation and trigger apoptosis.
While PERK complexes shift to large complexes, ATF6alpha complexes are reduced to smaller complexes on endoplasmic reticulum (ER) stress. In contrast, IRE1alpha complexes were not significantly increased in size on ER stress, unless IRE1alpha is overexpressed.
Increased PERK-specific endoplasmic reticulum stress signaling is in response to overstretch in ventilator-induced lung injury.
phosphorylated PERK and ATF4 would be upregulated in Orexin neurons in Sudden Infant Death Syndrome (SIDS) compared to non-SIDS.
In this paper, we evaluate the clinical features of the patients having W522X mutation and we compare this group with other patients reported to date. Except the characteristic features as diabetes mellitus and epiphyseal dysplasia, all the WRS patients, including patients with W522X mutation, show extensive phenotypic variability that correlates poorly to genotype.
PERK is a master-regulator dictating pancreatic beta cell homoeostasis in development and in diabetes. (Review)
Three branches of the Unfolded Protein Response (UPR) have been described, including the activation of the inositol-requiring enzyme 1 (IRE1), the pancreatic ER kinase (PKR)-like ER kinase (PERK), and the activating transcription factor 6 (ATF6).
Our work demonstrates for the first time that the adaptation to endoplasmic reticulum(ER) stress in cancer cells produces a MDR phenotype. The PERK/Nrf2/MRP1 axis is responsible for the resistance to ER stress and chemotherapy, and may represent a good therapeutic target in aggressive and resistant tumors.
miR-204 Targets PERK and Regulates UPR Signaling and beta-Cell Apoptosis
novel findings suggest that HMGB1 triggered EPC apoptosis in a manner of RAGE-mediated activation of the PERK/eIF2alpha pathway.
The protein encoded by this gene phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2 (EIF2), leading to its inactivation, and thus to a rapid reduction of translational initiation and repression of global protein synthesis. It is a type I membrane protein located in the endoplasmic reticulum (ER), where it is induced by ER stress caused by malfolded proteins. Mutations in this gene are associated with Wolcott-Rallison syndrome.
eukaryotic translation initiation factor 2-alpha kinase 3
, eukaryotic translation initiation factor 2-alpha kinase 3-like
, PRKR-like endoplasmic reticulum kinase
, pancreatic eIF2-alpha kinase
, eukaryotic translation initiation factor 2 alpha kinase 3
, pancreatic EIF2-alpha kinase