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the impaired working memory in forebrain-specific Perk knockout mice may stem from altered Gq protein-coupled intracellular Ca(2 (show CA2 Proteins)+) dynamics in cortical pyramidal neurons.
Overall, these data demonstrate that hypoxia can suppress adiponectin (show ADIPOQ PLURAL_@37961@) expression and activate the PERK and IRE1 (show ERN1 PLURAL_@37961@) signaling pathways in differentiated adipocytes, and this two pathways are involved in the suppression of adiponectin (show ADIPOQ PLURAL_@37961@) expression induced by hypoxia.
Free CNPY2 (show CNPY2 Proteins) then engages protein kinase (show CDK7 Proteins) R-like endoplasmic reticulum kinase (PERK) to induce expression of the transcription factor C/EBP homologous protein (CHOP (show DDIT3 Proteins)), thereby initiating the unfolded protein response.
Therefore, our study suggests that CREB and PSD95 are novel substrates of PERK, so inhibition of PERK phosphorylation using GSK2656157 would be beneficial against memory impairment after TBI.
regulates both Ca2 (show CA2 Proteins)+ -dependent working memory and protein synthesis-dependent memory flexibility
SLC30A10 (show SLC30A10 Proteins) has a protective role in 1-methyl-4-phenylpyridinium-induced toxicity via PERK-ATF4 (show ATF4 Proteins) pathway.
In many endoplasmic reticulum (ER) stress-related disorders, activation of the unfolded protein sensor protein kinase RNA-like ER kinase (PERK) kinase is beneficial. Nonetheless, in Charcot-Marie-Tooth 1B neuropathy mice, we show that activation of PERK in Schwann cells, but not in neurons, is detrimental for myelination. PERK may interfere with myelination, independent of its role in ER stress.
ER-stressed astrocytes can drive an inflammatory M1-like phenotype in microglia, and this can be attenuated with inhibition of PERK. Importantly, targeting PERK neither disrupted normal cytokine signaling in astrocytes or microglia nor impaired macrophage phagocytosis or T cell polarization.
These results suggest that PERK signaling promotes medulloblastoma tumorigenesis by attenuating apoptosis of premalignant granule cell precursors during the course of malignant transformation.
These results suggest that the PERK arm of the unfolded protein response plays a pivotal role in the regulation of satellite cell homeostasis during regenerative myogenesis.
To illustrate the mechanism by which the PERK luminal domain interacts with misfolded proteins, the crystal structure of the human PERK luminal domain was determined to 3.2 A resolution. Two dimers of the PERK luminal domain constitute a tetramer in the asymmetric unit.
These results indicated that dual targeting of PI3K and PERK pathways might improve clinical prognosis and enhance the treatment of ESCC patients.
The role of neutrophil elastase (show ELANE Proteins) in the activation of unfolded protein response effector molecules via PERK and CHOP (show DDIT3 Proteins) is reported.
High PERK expression is associated with gastrointestinal neuroendocrine tumors.
The PERK-eIF2alpha (show EIF2A Proteins)-ATF4 (show ATF4 Proteins)-CHOP (show DDIT3 Proteins) signaling pathway has a critical role in tumor progression during endoplasmic reticulum stress. (Review)
Results unveil a new aspect of PERK function and previously unknown roles for Claspin and Chk1 (show CHEK1 Proteins) as negative regulators of DNA replication in the absence of genotoxic stress.
These data indicate that PERK regulates radioresistance in oropharyngeal carcinoma through NF-kB activation-mediated phosphorylation of eIF2alpha (show EIF2A Proteins)
The actin regulator FLNA interacts with the endoplasmic reticulum stress kinase PERK and this interaction is required for the efficient formation of ER-plasma membrane contact sites.
SLC30A10 has a protective role in 1-methyl-4-phenylpyridinium-induced toxicity via PERK-ATF4 (show ATF4 Proteins) pathway.
We reveal distinct binding affinities between the binary and ternary complexes thus formed, that suggest a preference for the PERK signaling branch under stress, and a predilection for the GRP78 (show HSPA5 Proteins)-UPR sensor complex formation upon stressor removal. These results imply a gated UPR mechanism that tunes the overall cellular behavior to the accumulation of unfolded proteins.
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