Eif2ak4 binds tRNA

Stable Identifier
R-MMU-9633481
Type
Reaction [binding]
Species
Mus musculus
Compartment
ReviewStatus
5/5
General
SVG |   | PPTX  | SBGN
Eif2ak4 binds tRNA
The histidyl-tRNA synthetase domain in the C-terminal region of Eif2ak4 (Gcn2) binds uncharged tRNA (inferred from yeast homologs). Gcn1 and Eif2ak4 interact with translating ribosomes (Roffe et al. 2013) and with each other (Cambiaghi et al. 2014), though the interaction between mouse Eif2ak4 and ribosomes is not as stable as the interaction between yeast GCN2 and ribosomes. The interaction between Gcn1 and Eif2ak4 is required for activation of Atf4 and Chop by Eif2ak4 (Cambiaghi et al. 2014).
Literature References
PubMed ID Title Journal Year
26526991 Re-examination of Dietary Amino Acid Sensing Reveals a GCN2-Independent Mechanism

Leib, DE, Knight, ZA

Cell Rep 2015
24333428 Evolutionarily conserved IMPACT impairs various stress responses that require GCN1 for activating the eIF2 kinase GCN2

Pereira, CM, Shanmugam, R, Sattlegger, E, Wek, RC, Bolech, M, Castilho, BA, Cambiaghi, TD

Biochem. Biophys. Res. Commun. 2014
23447528 IMPACT is a developmentally regulated protein in neurons that opposes the eukaryotic initiation factor 2α kinase GCN2 in the modulation of neurite outgrowth

Alves, VS, Roffé, M, Hajj, GN, Azevedo, HF, Castilho, BA

J. Biol. Chem. 2013
24719324 Crystal structures of GCN2 protein kinase C-terminal domains suggest regulatory differences in yeast and mammals

Dey, S, Georgiadis, MM, Wek, RC, He, H, Baird, TD, Wek, SA, Singh, I

J. Biol. Chem. 2014
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