ArticleThe Journal of biological chemistry2019
Ablation of elongation factor 2 kinase enhances heat-shock protein 90 chaperone expression and protects cells under proteotoxic stress.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- Targeting proteostasis for cancer therapy: current advances, challenges, and future perspectives.Molecular cancer · 2025Review
- The mex-3 3' untranslated region is essential for reproduction during temperature stress.Development (Cambridge, England) · 2025Article
- Elongation factor-2 kinase is a critical determinant of the fate and antitumor immunity of CD8Science advances · 2022Article
- Potential predictive value of plasma heat shock protein 90α in lung cancer.The Journal of international medical research · 2021Article
- Integrative proteomics reveals the role of E3 ubiquitin ligase SYVN1 in hepatocellular carcinoma metastasis.Cancer communications (London, England) · 2021Article
- Advances in the role and mechanism of BAG3 in dilated cardiomyopathy.Heart failure reviews · 2021Review
- Proteome Turnover in the Spotlight: Approaches, Applications, and Perspectives.Molecular & cellular proteomics : MCP · 2021Review
- Quinolinate as a Marker for Kynurenine Metabolite Formation and the Unresolved Question of NADFrontiers in immunology · 2020Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic elongation factor 2 kinase (eEF2K) negatively regulates the elongation stage of mRNA translation and is activated under different stress conditions to slow down protein synthesis. One effect of eEF2K is to alter the repertoire of expressed proteins, perhaps to aid survival of stressed cells. Here, we applied pulsed stable isotope labeling with amino acids in cell culture (SILAC) to study changes in the synthesis of specific proteins in human lung adenocarcinoma (A549) cells in which eEF2K had been depleted by an inducible shRNA. We discovered that levels of heat-shock protein 90 (HSP90) are increased in eEF2K-depleted human cells as well as in eEF2K-knockout (eEF2K
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