Dec 25, 2024 · GCN1 (GCN1 Activator Of EIF2AK4) is a Protein Coding gene. Diseases associated with GCN1 include Ogden Syndrome and Pulmonary Interstitial Emphysema. Among its related pathways are Cellular responses to stimuli and Peptide chain elongation. An important paralog of this gene is ECPAS.

Gcn1-ribosome co-sedimentation assays suggest that Gcn20 modulates the affinity of Gcn1 to the ribosome, supporting the idea that Gcn20 fine-tunes Gcn1-ribosome interaction in response to certain non-yet-known conditions, and that way may modulate the level of …

Jun 1, 2024 · GCN1 is a highly conserved protein present widely across eukaryotes. As an upstream activator of protein kinase GCN2, GCN1 plays a pivotal role in integrated stress responses, such as amino acid starvation and oxidative stress.

Jan 12, 2023 · GCN1 is a conserved ribosome-associated scaffolding protein that binds the RWD domain of the integrated stress response kinase, GCN2. 46, 47 In addition, GCN1 was recently shown to interact with collided, elongation-stalled ribosomes in yeast 20 and human cells, 21 although the relative binding affinities of GCN1 for monosomes vs. disomes ...

Apr 23, 2020 · Here, we show that GCN1 is involved in GCN2-mediated eIF2α phosphorylation after AAS and UV radiation by generating Gcn1 mutant mice. Interestingly, GCN1 not only regulates the eIF2α-mediated stress response but also the cell cycle and cell proliferation in a GCN2-independent manner.

Apr 23, 2020 · GCN1 is a GCN2-binding protein that possesses an RWD binding domain (RWDBD) in its C-terminus. In yeast, Gcn1 is essential for Gcn2 activation by AAS; however, the roles of GCN1 in mammals need to be established.

Jun 19, 2023 · GCN1 then recruits CCR4/NOT and other quality control factors, shaping global mRNA turnover. These results position GCN1 as a key translational regulator of proteostasis, a function with increasing importance in adjusting translational dynamics during aging.

Feb 9, 2025 · These findings suggest that GCN1 can regulate eIF2alpha phosphorylation in HSV-1-infected cells and that the GCN1-binding viral partner simplexvirus gH is necessary and sufficient to prevent the accumulation of phosphorylated eIF2alpha.

The GCN1-GCN20 complex interacts with GCN2 on translating ribosomes in amino acid-starved cells; GCN1 may bind near the ribosomal A-site and promotes the transfer of uncharged tRNAs from the A-site to the tRNA-binding domain in GCN2 for its subsequent kinase activation, and hence allowing GCN4 translational activation and derepression of amino ...

GCN2 stimulates GCN4 translation in amino acid-starved cells by phosphorylating the α-subunit of translation initiation factor 2. GCN2 function in vivo requires the GCN1/GCN20 complex, which binds to the N-terminal domain of GCN2. A C-terminal ...