Separate domains in GCN1 for binding protein kinase GCN2 and ribosomes are required for GCN2 activation in amino acid-starved cells.
about
Binding of cellular p32 protein to the rubella virus P150 replicase protein via PxxPxR motifsYeast studies reveal moonlighting functions of the ancient actin cytoskeletonCell growth control by stable Rbg2/Gir2 complex formation under amino acid starvation.Gcn1 and actin binding to Yih1: implications for activation of the eIF2 kinase GCN2.YIH1 is an actin-binding protein that inhibits protein kinase GCN2 and impairs general amino acid control when overexpressed.Polyribosome binding by GCN1 is required for full activation of eukaryotic translation initiation factor 2{alpha} kinase GCN2 during amino acid starvation.Evidence that Yih1 resides in a complex with ribosomes.Saccharomyces cerevisiae Rbg1 protein and its binding partner Gir2 interact on Polyribosomes with Gcn1.Evidence that eukaryotic translation elongation factor 1A (eEF1A) binds the Gcn2 protein C terminus and inhibits Gcn2 activityGcn1 contacts the small ribosomal protein Rps10, which is required for full activation of the protein kinase Gcn2.Overexpression of eukaryotic translation elongation factor 3 impairs Gcn2 protein activation.IMPACT, a protein preferentially expressed in the mouse brain, binds GCN1 and inhibits GCN2 activationRecognition of a structural domain (RWDBD) in Gcn1 proteins that interacts with the RWD domain containing proteins.Enhanced interaction between pseudokinase and kinase domains in Gcn2 stimulates eIF2α phosphorylation in starved cellstRNAs as regulators of biological processesArginase II restricts host defense to Helicobacter pylori by attenuating inducible nitric oxide synthase translation in macrophagesThe inhibition of protein translation mediated by AtGCN1 is essential for cold tolerance in Arabidopsis thalianaGcn4p, a master regulator of gene expression, is controlled at multiple levels by diverse signals of starvation and stress.Structural basis for autoinhibition and mutational activation of eukaryotic initiation factor 2alpha protein kinase GCN2.Differential activation of eIF2 kinases in response to cellular stresses in Schizosaccharomyces pombe.IMPACT is a GCN2 inhibitor that limits lifespan in Caenorhabditis elegans.Translational control of inducible nitric oxide synthase expression by arginine can explain the arginine paradox.Interaction between the tRNA-binding and C-terminal domains of Yeast Gcn2 regulates kinase activity in vivo.The Gcn2 Regulator Yih1 Interacts with the Cyclin Dependent Kinase Cdc28 and Promotes Cell Cycle Progression through G2/M in Budding Yeast.Mutations that bypass tRNA binding activate the intrinsically defective kinase domain in GCN2.L-arginine availability regulates inducible nitric oxide synthase-dependent host defense against Helicobacter pylori.GCN-2 dependent inhibition of protein synthesis activates osmosensitive gene transcription via WNK and Ste20 kinase signaling.Solution structure of the RWD domain of the mouse GCN2 proteinSemaphorin controls epidermal morphogenesis by stimulating mRNA translation via eIF2alpha in Caenorhabditis elegans.Eukaryotic initiation factor 2 phosphorylation and translational control in metabolism.Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae.Changes in translation rate modulate stress-induced damage of diverse proteins.Role of Eukaryotic Initiation Factors during Cellular Stress and Cancer ProgressionThe unique role of dietary L-arginine in the acceleration of peritoneal macrophage sensitivity to bacterial endotoxin.Eukaryotic translation initiation factors and cancer.Activation of Gcn2 in response to different stresses.G-protein control of the ribosome-associated stress response protein SpoT.Parasite-specific eIF2 (eukaryotic initiation factor-2) kinase required for stress-induced translation control.Serine 577 is phosphorylated and negatively affects the tRNA binding and eIF2alpha kinase activities of GCN2.EIF2AK4 mutations cause pulmonary veno-occlusive disease, a recessive form of pulmonary hypertension.
P2860
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P2860
Separate domains in GCN1 for binding protein kinase GCN2 and ribosomes are required for GCN2 activation in amino acid-starved cells.
description
2000 nî lūn-bûn
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2000 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
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2000 թվականի դեկտեմբերին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年论文
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name
Separate domains in GCN1 for b ...... n in amino acid-starved cells.
@ast
Separate domains in GCN1 for b ...... n in amino acid-starved cells.
@en
Separate domains in GCN1 for b ...... n in amino acid-starved cells.
@nl
type
label
Separate domains in GCN1 for b ...... n in amino acid-starved cells.
@ast
Separate domains in GCN1 for b ...... n in amino acid-starved cells.
@en
Separate domains in GCN1 for b ...... n in amino acid-starved cells.
@nl
prefLabel
Separate domains in GCN1 for b ...... n in amino acid-starved cells.
@ast
Separate domains in GCN1 for b ...... n in amino acid-starved cells.
@en
Separate domains in GCN1 for b ...... n in amino acid-starved cells.
@nl
P2860
P3181
P356
P1433
P1476
Separate domains in GCN1 for b ...... n in amino acid-starved cells.
@en
P2093
A G Hinnebusch
E Sattlegger
P2860
P304
P3181
P356
10.1093/EMBOJ/19.23.6622
P407
P577
2000-12-01T00:00:00Z