Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

PLoS genetics - 1 Feb 2015

Lageix Sebastien, Zhang Jinwei, Rothenburg Stefan, Hinnebusch Alan G

Abstract excerpt

The stress-activated protein kinase Gcn2 regulates protein synthesis by phosphorylation of translation initiation factor eIF2α. Gcn2 is activated in amino acid-deprived cells by binding of uncharged tRNA to the regulatory domain related to histidyl-tRNA synthetase, but the molecular mechanism of activation is unclear. We used a genetic approach to identify a key regulatory surface in Gcn2 that is proximal to the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Substitution
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Eukaryotic Initiation Factor-2

Share to Protein Conformation

Share to Protein Serine-Threonine Kinases

Share to RNA, Transfer

Share to Saccharomyces cerevisiae Proteins

Share to Trypanosoma cruzi

Source

Open in PubMed Open full text

Identifiers

PMID: 25695491
DOI: 10.1371/journal.pgen.1004991
PMCID: PMC4335047

Provenance

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

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Interaction between the tRNA-binding and C-terminal domains of Yeast Gcn2 regulates kinase activity in vivo.PMID 25695491Read ↗

Mutations that bypass tRNA binding activate the intrinsically defective kinase domain in GCN2.Semantic proximity Read ↗

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

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

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

A network of hydrophobic residues impeding helix alphaC rotation maintains latency of kinase Gcn2, which phosphorylates the alpha subunit of translation initiation factor 2.Semantic proximity Read ↗

Structural basis for autoinhibition and mutational activation of eukaryotic initiation factor 2alpha protein kinase GCN2.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 ↗

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

Association of GCN1-GCN20 regulatory complex with the N-terminus of eIF2alpha kinase GCN2 is required for GCN2 activation.Semantic proximity Read ↗

Selective control of amino acid metabolism by the GCN2 eIF2 kinase pathway in Saccharomyces cerevisiae.Semantic proximity Read ↗

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

⌁Select a neighboring publication to make it the new centre.