Evidence that Yih1 resides in a complex with ribosomes

No abstract is available for this paper.

• Publication year

  2012

• Venue

  The FEBS Journal

• Publication date

  2012-05-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1111/j.1742-4658.2012.08553.xPMID 22404850
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Gcn1 and Actin Binding to Yih1

  2011cited by this paper
• Evidence That Eukaryotic Translation Elongation Factor 1A (eEF1A) Binds the Gcn2 Protein C Terminus and Inhibits Gcn2 Activity*♦

  2011cited by this paper
• Yeast studies reveal new roles for an ancient skeleton

  2009cited by this paper
• Saccharomyces cerevisiae Rbg1 Protein and Its Binding Partner Gir2 Interact on Polyribosomes with Gcn1

  2009cited by this paper
• Utility of formaldehyde cross-linking and mass spectrometry in the study of protein-protein interactions.

  2008cited by this paper
• Rwdd1, a Thymus Aging Related Molecule, Is a New Member of the Intrinsically Unstructured Protein Family

  2008cited by this paper
• Antiviral effect of the mammalian translation initiation factor 2α kinase GCN2 against RNA viruses

  2006cited by this paper
• The Combined Effects of Tryptophan Starvation and Tryptophan Catabolites Down-Regulate T Cell Receptor ζ-Chain and Induce a Regulatory Phenotype in Naive T Cells1

  2006cited by this paper
• Translational control of hippocampal synaptic plasticity and memory by the eIF2α kinase GCN2

  2005cited by this paper
• IMPACT, a Protein Preferentially Expressed in the Mouse Brain, Binds GCN1 and Inhibits GCN2 Activation*

  2005cited by this paper
• Translational regulation of GCN4 and the general amino acid control of yeast.

  2005cited by this paper
• Polyribosome Binding by GCN1 Is Required for Full Activation of Eukaryotic Translation Initiation Factor 2α Kinase GCN2 during Amino Acid Starvation*

  2005cited by this paper
• The GCN2 kinase biases feeding behavior to maintain amino acid homeostasis in omnivores.

  2005cited by this paper
• Uncharged tRNA and Sensing of Amino Acid Deficiency in Mammalian Piriform Cortex

  2005cited by this paper
• Gir2 is an intrinsically unstructured protein that is present in Saccharomyces cerevisiae as a group of heterogeneously electrophoretic migrating forms.

  2005cited by this paper
• Phosphorylation of eIF2alpha is involved in the signaling of indispensable amino acid deficiency in the anterior piriform cortex of the brain in rats.

  2004cited by this paper
• Biophysical characterization of Gir2, a highly acidic protein of Saccharomyces cerevisiae with anomalous electrophoretic behavior.

  2004cited by this paper
• YIH1 Is an Actin-binding Protein That Inhibits Protein Kinase GCN2 and Impairs General Amino Acid Control When Overexpressed*

  2004cited by this paper
• Global analysis of protein expression in yeast

  2003cited by this paper
• Functional Interactions between Yeast Translation Eukaryotic Elongation Factor (eEF) 1A and eEF3*

  2003cited by this paper
• 5 Mechanism and Regulation of Initiator Methionyl-tRNA Binding to Ribosomes

  2000cited by this paper
• GI Domain-mediated Association of the Eukaryotic Initiation Factor 2α Kinase GCN2 with Its Activator GCN1 Is Required for General Amino Acid Control in Budding Yeast*

  2000cited by this paper
• Separate domains in GCN1 for binding protein kinase GCN2 and ribosomes are required for GCN2 activation in amino acid‐starved cells

  2000cited by this paper
• Evidence that GCN1 and GCN20, translational regulators of GCN4, function on elongating ribosomes in activation of eIF2alpha kinase GCN2

  1997cited by this paper
• A new efficient gene disruption cassette for repeated use in budding yeast

  1996cited by this paper
• GCN20, a novel ATP binding cassette protein, and GCN1 reside in a complex that mediates activation of the eIF‐2 alpha kinase GCN2 in amino acid‐starved cells.

  1995cited by this paper
• The Elongation Factor 3 Unique in Higher Fungi and Essential for Protein Biosynthesis Is an E Site Factor (*)

  1995cited by this paper
• Comparative analysis of ribosome-associated adenosinetriphosphatase (ATPase) from pig liver and the ATPase of elongation factor 3 from Saccharomyces cerevisiae.

  1994cited by this paper
• Ultrastructure of the yeast actin cytoskeleton and its association with the plasma membrane

  1994cited by this paper
• PUB1 is a major nuclear and cytoplasmic polyadenylated RNA-binding protein in Saccharomyces cerevisiae

  1993cited by this paper
• GCN1, a translational activator of GCN4 in Saccharomyces cerevisiae, is required for phosphorylation of eukaryotic translation initiation factor 2 by protein kinase GCN2

  1993cited by this paper
• Phosphorylation of initiation factor 2α by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast

  1992cited by this paper
• GCD2, a translational repressor of the GCN4 gene, has a general function in the initiation of protein synthesis in Saccharomyces cerevisiae

  1991cited by this paper
• Ribosome association of GCN2 protein kinase, a translational activator of the GCN4 gene of Saccharomyces cerevisiae.

  1991cited by this paper
• Uncharged tRNA, protein synthesis, and the bacterial stringent response

  1990cited by this paper
• A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae.

  1989cited by this paper
• Escherichia Coli and Salmonella: Typhimurium Cellular and Molecular Biology

  1987cited by this paper
• On Stringent Response

  1972cited by this paper
• Mode of action of the herbicide, 3-amino-1,2,4-triazole(amitrole): inhibition of an enzyme of histidine biosynthesis.

  1965cited by this paper

• Conserved genetic basis for microbial colonization of the gut.

  2025cites this paper
• Mutational analysis of Yih1 and IMPACT reveals amino acids required for Gcn2 inhibition

  2025cites this paper
• Oxidative stress‐induced YAP1 expression is regulated by NCE102, CDA2, and BCS1

  2024cites this paper
• Emerging Role of GCN1 in Disease and Homeostasis

  2024cites this paper
• Evidence that Xrn1 is in complex with Gcn1, and is required for full levels of eIF2α phosphorylation

  2024cites this paper
• Spinal cord injury regulates circular RNA expression in axons

  2023cites this paper
• Asp56 in actin is critical for the full activity of the amino acid starvation‐responsive kinase Gcn2

  2021cites this paper
• Yeast as a Model to Understand Actin-Mediated Cellular Functions in Mammals—Illustrated with Four Actin Cytoskeleton Proteins

  2020cites this paper
• Experimentally based structural model of Yih1 provides insight into its function in controlling the key translational regulator Gcn2

  2020cites this paper
• The Leishmania donovani IMPACT-like protein possesses non-specific nuclease activity.

  2018cites this paper
• Perturbations in actin dynamics reconfigure protein complexes that modulate GCN2 activity and promote an eIF2 response

  2016cites this paper
• Gcn1 contacts the small ribosomal protein Rps10, which is required for full activation of the protein kinase Gcn2.

  2015cites this paper
• The Gcn2 Regulator Yih1 Interacts with the Cyclin Dependent Kinase Cdc28 and Promotes Cell Cycle Progression through G2/M in Budding Yeast

  2015cites this paper
• Semi-quantitative colony immunoassay for determining and optimizing protein expression in Saccharomyces cerevisiae and Escherichia coli.

  2014cites this paper
• Keeping the eIF2 alpha kinase Gcn2 in check.

  2014influential citation
• Evolutionarily conserved IMPACT impairs various stress responses that require GCN1 for activating the eIF2 kinase GCN2.

  2014cites this paper
• IMPACT Is a Developmentally Regulated Protein in Neurons That Opposes the Eukaryotic Initiation Factor 2α Kinase GCN2 in the modulation of Neurite Outgrowth*

  2013cites this paper
• Shedding light on the link between the actin cytoskeleton and stress response in Saccharomyces cerevisiae : a thesis submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy in Biochemistry, Massey University, Auckland, New Zealand

  2012cites this paper