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Article

YIH1 is an actin-binding protein that inhibits protein kinase GCN2 and impairs general amino acid control when overexpressed.

The Journal of biological chemistry - 16 Jul 2004

Sattlegger Evelyn, Swanson Mark J, Ashcraft Emily A, Jennings Jennifer L, Fekete Richard A, Link Andrew J, Hinnebusch Alan G

Abstract excerpt

The general amino acid control (GAAC) enables yeast cells to overcome amino acid deprivation by activation of the alpha subunit of translation initiation factor 2 (eIF2alpha) kinase GCN2 and consequent induction of GCN4, a transcriptional activator of amino acid biosynthetic genes. Binding of GCN2 to GCN1 is required for stimulation of GCN2 kinase activity by uncharged tRNA in starved cells. Here we show that...

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Source

Identifiers

PMID: 15126500
DOI: 10.1074/jbc.M404009200

Genes

GCN1

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

YIH1 is an actin-binding protein that inhibits protein kinase GCN2 and impairs general amino acid control when overexpressed.PMID 15126500Read ↗

GI domain-mediated association of the eukaryotic initiation factor 2alpha kinase GCN2 with its activator GCN1 is required for general amino acid control in budding yeast.Semantic proximity Read ↗

Asp56 in actin is critical for the full activity of the amino acid starvation-responsive kinase Gcn2.Semantic proximity Read ↗

Budding yeast GCN1 binds the GI domain to activate the eIF2alpha kinase GCN2.Semantic proximity Read ↗

GCN1, a translational activator of GCN4 in Saccharomyces cerevisiae, is required for phosphorylation of eukaryotic translation initiation factor 2 by protein kinase GCN2.Semantic proximity Read ↗

Identification of positive-acting domains in GCN2 protein kinase required for translational activation of GCN4 expression.Semantic proximity Read ↗

Experimentally based structural model of Yih1 provides insight into its function in controlling the key translational regulator Gcn2.Semantic proximity Read ↗

Interaction between the tRNA-binding and C-terminal domains of Yeast Gcn2 regulates kinase activity in vivo.Semantic proximity Read ↗

The yeast eIF4E-associated protein Eap1p attenuates GCN4 translation upon TOR-inactivation.Semantic proximity Read ↗

Crystal structures of GCN2 protein kinase C-terminal domains suggest regulatory differences in yeast and mammals.Semantic proximity Read ↗

Mutations activating the yeast eIF-2 alpha kinase GCN2: isolation of alleles altering the domain related to histidyl-tRNA synthetases.Semantic proximity Read ↗

Overexpression of eukaryotic translation elongation factor 3 impairs Gcn2 protein activation.Semantic proximity Read ↗

Genetic and biochemical evidence for yeast GCN2 protein kinase polymerization.Semantic proximity Read ↗

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