Dimerization by translation initiation factor 2 kinase GCN2 is mediated by interactions in the C-terminal ribosome-binding region and the protein kinase domain.
about
A mammalian homologue of GCN2 protein kinase important for translational control by phosphorylation of eukaryotic initiation factor-2alphaAssociation of GCN1-GCN20 regulatory complex with the N-terminus of eIF2alpha kinase GCN2 is required for GCN2 activationHost cell manipulation by the human pathogen Toxoplasma gondiiGenome-wide analysis of tRNA charging and activation of the eIF2 kinase Gcn2pIfkA, a presumptive eIF2 alpha kinase of Dictyostelium, is required for proper timing of aggregation and regulation of mound sizeEukaryotic initiation factor (eIF) 1 carries two distinct eIF5-binding faces important for multifactor assembly and AUG selectionCrystal Structures of GCN2 Protein Kinase C-terminal Domains Suggest Regulatory Differences in Yeast and MammalsMultiple elements in the eIF4G1 N-terminus promote assembly of eIF4G1•PABP mRNPs in vivo.Evidence that eukaryotic translation elongation factor 1A (eEF1A) binds the Gcn2 protein C terminus and inhibits Gcn2 activityTwo heme-binding domains of heme-regulated eukaryotic initiation factor-2alpha kinase. N terminus and kinase insertionEnhanced interaction between pseudokinase and kinase domains in Gcn2 stimulates eIF2α phosphorylation in starved cellsConserved bipartite motifs in yeast eIF5 and eIF2Bepsilon, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2.Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the alpha subunit of eukaryotic translation initiation factor 2 [corrected]Glucose limitation induces GCN4 translation by activation of Gcn2 protein kinase.Heterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR.Structural basis for autoinhibition and mutational activation of eukaryotic initiation factor 2alpha protein kinase GCN2.The tRNA-binding moiety in GCN2 contains a dimerization domain that interacts with the kinase domain and is required for tRNA binding and kinase activation.Conserved intermolecular salt bridge required for activation of protein kinases PKR, GCN2, and PERK.Interaction between the tRNA-binding and C-terminal domains of Yeast Gcn2 regulates kinase activity in vivo.A GCN2-like eukaryotic initiation factor 2 kinase increases the viability of extracellular Toxoplasma gondii parasites.Mutations that bypass tRNA binding activate the intrinsically defective kinase domain in GCN2.Mechanisms regulating the protein kinases of Saccharomyces cerevisiae.Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae.Receptor for activated C-kinase (RACK1) homolog Cpc2 facilitates the general amino acid control response through Gcn2 kinase in fission yeastA network of hydrophobic residues impeding helix alphaC rotation maintains latency of kinase Gcn2, which phosphorylates the alpha subunit of translation initiation factor 2.Old target new approach: an alternate NF-kappaB activation pathway via translation inhibition.GCN2-like eIF2α kinase manages the amino acid starvation response in Toxoplasma gondii.Kynurenine metabolism in health and disease.cpc-3, the Neurospora crassa homologue of yeast GCN2, encodes a polypeptide with juxtaposed eIF2alpha kinase and histidyl-tRNA synthetase-related domains required for general amino acid control.eIF2α kinases control chalone production in Dictyostelium discoideum.Regulation of PKR by RNA: formation of active and inactive dimers.Regulation of internal ribosome entry site-mediated translation by eukaryotic initiation factor-2alpha phosphorylation and translation of a small upstream open reading frame.Yeast Mpk1 mitogen-activated protein kinase activates transcription through Swi4/Swi6 by a noncatalytic mechanism that requires upstream signal.Serine 577 is phosphorylated and negatively affects the tRNA binding and eIF2alpha kinase activities of GCN2.Functional mapping of Bas2. Identification of activation and Bas1-interaction domains.Dimerization is required for activation of eIF2 kinase Gcn2 in response to diverse environmental stress conditions.Nck-1 selectively modulates eIF2alphaSer51 phosphorylation by a subset of eIF2alpha-kinases.
P2860
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P2860
Dimerization by translation initiation factor 2 kinase GCN2 is mediated by interactions in the C-terminal ribosome-binding region and the protein kinase domain.
description
1998 nî lūn-bûn
@nan
1998 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Dimerization by translation in ...... and the protein kinase domain.
@ast
Dimerization by translation in ...... and the protein kinase domain.
@en
Dimerization by translation in ...... and the protein kinase domain.
@nl
type
label
Dimerization by translation in ...... and the protein kinase domain.
@ast
Dimerization by translation in ...... and the protein kinase domain.
@en
Dimerization by translation in ...... and the protein kinase domain.
@nl
prefLabel
Dimerization by translation in ...... and the protein kinase domain.
@ast
Dimerization by translation in ...... and the protein kinase domain.
@en
Dimerization by translation in ...... and the protein kinase domain.
@nl
P2093
P2860
P356
P1476
Dimerization by translation in ...... and the protein kinase domain.
@en
P2093
A G Hinnebusch
M T Garcia-Barrio
P2860
P304
P356
10.1128/MCB.18.5.2697
P407
P577
1998-05-01T00:00:00Z