Dimerization and release of molecular chaperone inhibition facilitate activation of eukaryotic initiation factor-2 kinase in response to endoplasmic reticulum stress (Q24292499)

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English	Dimerization and release of molecular chaperone inhibition facilitate activation of eukaryotic initiation factor-2 kinase in response to endoplasmic reticulum stress	scientific article

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scholarly article

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Dimerization and release of molecular chaperone inhibition facilitate activation of eukaryotic initiation factor-2 kinase in response to endoplasmic reticulum stress (English)

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endoplasmic reticulum

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molecular chaperones

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Eukaryotic translation initiation factor 2 alpha kinase 3

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GOA release 2020-03-11

protein autophosphorylation

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GOA release 2020-03-11

author name string

Kun Ma

1

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Krishna M Vattem

2

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Ronald C Wek

3

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language of work or name

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publication date

24 May 2002

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Journal of Biological Chemistry

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277

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21

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18728-35

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eIF-2 kinases: regulators of general and gene-specific translation initiation

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PKR: a new name and new roles.

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Double-stranded RNA-activated protein kinase mediates virus-induced apoptosis: a new role for an old actor

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PKR; a sentinel kinase for cellular stress

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Heme-regulated eIF2alpha kinase (HRI) is required for translational regulation and survival of erythroid precursors in iron deficiency

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Characterization of a mammalian homolog of the GCN2 eukaryotic initiation factor 2alpha kinase

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Regulated translation initiation controls stress-induced gene expression in mammalian cells

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Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control

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Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase

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21 January 2018

Pancreatic eukaryotic initiation factor-2alpha kinase (PEK) homologues in humans, Drosophila melanogaster and Caenorhabditis elegans that mediate translational control in response to endoplasmic reticulum stress

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Perk is essential for translational regulation and cell survival during the unfolded protein response

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Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls

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Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation

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Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase

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A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus

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A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells

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Cloning of mammalian Ire1 reveals diversity in the ER stress responses

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Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development

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Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum

1 reference

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EIF2AK3, encoding translation initiation factor 2-alpha kinase 3, is mutated in patients with Wolcott-Rallison syndrome

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Hsp90 is obligatory for the heme-regulated eIF-2alpha kinase to acquire and maintain an activable conformation.

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Dual role for Hsc70 in the biogenesis and regulation of the heme-regulated kinase of the alpha subunit of eukaryotic translation initiation factor 2

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Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response

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Dissociation of Kar2p/BiP from an ER sensory molecule, Ire1p, triggers the unfolded protein response in yeast

1 reference

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Characterization of phosphopeptides from protein digests using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and nanoelectrospray quadrupole time-of-flight mass spectrometry

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Mechanism of activation of the double-stranded-RNA-dependent protein kinase, PKR: role of dimerization and cellular localization in the stimulation of PKR phosphorylation of eukaryotic initiation factor-2 (eIF2).

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Histidyl-tRNA synthetase-related sequences in GCN2 protein kinase regulate in vitro phosphorylation of eIF-2.

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Inhibitory sequences in the N-terminus of the double-stranded-RNA-dependent protein kinase, PKR, are important for regulating phosphorylation of eukaryotic initiation factor 2alpha (eIF2alpha).

1 reference

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The unfolded protein response: an intracellular signalling pathway with many surprising features

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Homocysteine-dependent alterations in mitochondrial gene expression, function and structure. Homocysteine and H2O2 act synergistically to enhance mitochondrial damage

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Homocysteine induces programmed cell death in human vascular endothelial cells through activation of the unfolded protein response

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Translation initiation control by heme-regulated eukaryotic initiation factor 2alpha kinase in erythroid cells under cytoplasmic stresses

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Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the alpha subunit of eukaryotic translation initiation factor 2 [corrected]

1 reference

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The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR

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The interferon-inducible double-stranded RNA-activated protein kinase self-associates in vitro and in vivo

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Binding of double-stranded RNA to protein kinase PKR is required for dimerization and promotes critical autophosphorylation events in the activation loop.

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A dynamically tuned double-stranded RNA binding mechanism for the activation of antiviral kinase PKR.

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Autophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2alpha kinases PKR and GCN2

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Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus

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Regulation of translational initiation during cellular responses to stress

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Evidence that Hsc70 negatively modulates the activation of the heme-regulated eIF-2alpha kinase in rabbit reticulocyte lysate

1 reference

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based on heuristic

inferred from DOI database lookup

Ribosome targeting of PKR is mediated by two double-stranded RNA-binding domains and facilitates in vivo phosphorylation of eukaryotic initiation factor-2

1 reference

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based on heuristic

inferred from DOI database lookup

Immunoglobulin binding protein (BiP) function is required to protect cells from endoplasmic reticulum stress but is not required for the secretion of selective proteins

1 reference

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inferred from DOI database lookup

Identifiers

10.1074/JBC.M200903200

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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