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The nuclear cap-binding complex safeguards stress-resistant protein synthesis and proliferation of stem cells [Ribo-seq]

ABSTRACT: Various cellular stresses lead to an inhibition of steady-state translation driven by the cytoplasmic cap-binding protein eIF4E via the integrated stress response (ISR) in order to mitigate stress-induced damage. A caveat is that essential proteins for cell survival or maintenance should be expressed even under ISR-activated conditions. Here, we find that when global translation is compromised due to eIF2α phosphorylation during ISR, eIF2A takes over the function of eIF2α for Met-tRNAi delivery. Notably, preferential association between eIF2A and cellular factors involved in the pioneer round of translation driven by nuclear cap-binding protein complex (CBP20/80) allows the pioneer translation to occur during ISR. We also observe that ISR is activated in growing human embryonic stem cell (hESC) colonies. Under these naturally arising ISR conditions, eIF2A-mediated pioneer translation is active and safeguards self-renewal and differentiation of hESCs. Collectively, we unravel the molecular mechanism underlying translation that secures protein synthesis under cellular stress.

ORGANISM(S): Homo sapiens

PROVIDER: GSE225009 | GEO | 2026/03/30

REPOSITORIES: GEO

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Project description:CBP20 (Cap-Binding Protein 20) encodes a small subunit of the cap-binding complex (CBC), which is involved in the conserved cell processes related to RNA metabolism in plants and, simultaneously, engaged in the signaling network of drought response, which is dependent on ABA. CBP20 (Cap-Binding Protein 20), which encodes a small subunit of the cap-binding complex (CBC). CBC is a heterodimer that is formed by two subunits – a small one that is encoded by CBP20 and a large subunit that is encoded by CBP80 (Cap-Binding Protein 80). Both the nucleotide and amino acid sequences of CBP20 are highly conserved across species from Saccharomyces to Homo sapiens. CBP20 is involved in very conserved cell processes that are related to RNA metabolism such as polyadenylation and splicing, miRNA biogenesis, and according to the most recent reports, to histone methylation (Kuhn et al. 2008; Kim et al. 2008; Gregory et al. 2008; Kmieciak et al. 2002; Laubinger et al. 2008; Li et al. 2016). Most striking, however, is its simultaneous engagement in ABA signaling during seed germination and drought response (Papp et al. 2004; Jäger et al. 2011). It was shown that an Arabidopsis cbp20 mutant exhibited a hypersensitivity to ABA during seed germination and a better performance under water deficit conditions than the WT (Papp et al. 2004; Jäger et al. 2011). Interestingly, the Arabidopsis knockout mutant in CBP80 (Cap-Binding Protein 80; ABA hypersensitive 1) exhibited a similar phenotype when exposed to ABA or drought stress (Hugouvieux et al. 2001; 2002; Daszkowska-Golec et al. 2013). In Solanum tuberosum, an amiR80.2-14 mutant (CBP80 silenced using artificial microRNAs) was also reported to be drought tolerant (Pieczyński et al. 2013). Water-deficiency conditions related gene expression analysis was performed in barley in two genotypes: the wild-type (WT) barley cultivar 'Sebastian’ and hvcbp20.ab mutant; in three time points: (1) optimal water conditions, (2) onset of drought stress and (3) after 10 days of prolonged drought stress in the second leaf; analyses were performed in three biological replicates. Here, we report the enhanced tolerance to drought stress of barley mutant in the HvCBP20 gene.Transcriptome analysis using the Agilent Barley Microarray integrated with observed phenotypic traits allowed to conclude that the hvcbp20.ab mutant exhibited better fitness to stress conditions by its much more efficient and earlier activation of stress-preventing mechanisms. The network hubs involved in the adjustment of hvcbp20.ab mutant to the drought conditions were proposed. These results enabled to make a significant progress in understanding the role of CBP20 in the drought stress response.

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The nuclear cap-binding complex safeguards stress-resistant protein synthesis and proliferation of stem cells [Ribo-seq]

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