ArticleMolecular and cellular biology1998
Eukaryotic translation initiation factor 4G is targeted for proteolytic cleavage by caspase 3 during inhibition of translation in apoptotic cells.
Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.
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Who cites it
83 citing papers in PubMed, 195 citations in OpenAlex.
- Proteolytic dissection of eIF4G reveals the closed-loop mRNP as an architecture for translation repression.bioRxiv : the preprint server for biology · 2026Article
- Eukaryotic translation initiation factor 4F: functional properties and physiological role.Nucleic acids research · 2025Review
- Insight into the Life Cycle of Enterovirus-A71.Viruses · 2025Review
- Impaired interferon response in senecavirus A infection and identification of 3CJournal of virology · 2024Article
- Combined inhibition of KRASNature communications · 2024Article
- Cell death or survival: Insights into the role of mRNA translational control.Seminars in cell & developmental biology · 2024Review
- Mitochondrial DNA in cell death and inflammation.Biochemical Society transactions · 2023Review
- eIF4G has intrinsic G-quadruplex binding activity that is required for tiRNA function.Nucleic acids research · 2020Article
- Cellular Caspase-3 Contributes to EV-A71 2AVirologica Sinica · 2020Article
- Article
- Cap-Independent mRNA Translation in Germ Cells.International journal of molecular sciences · 2019Review
- Heterogeneity and specialized functions of translation machinery: from genes to organisms.Nature reviews. Genetics · 2018Review
- Human Rhinovirus 3C protease cleaves RIPK1, concurrent with caspase 8 activation.Scientific reports · 2018Article
- Heterogeneous nuclear ribonucleoprotein (hnRNP) L promotes DNA damage-induced cell apoptosis by enhancing the translation of p53.Oncotarget · 2017Article
- Norovirus-Mediated Modification of the Translational Landscape via Virus and Host-Induced Cleavage of Translation Initiation Factors.Molecular & cellular proteomics : MCP · 2017Article
- Global decay of mRNA is a hallmark of apoptosis in aging Xenopus eggs.RNA biology · 2017Article
- Proteasome inhibitors bortezomib and carfilzomib used for the treatment of multiple myeloma do not inhibit the serine protease HtrA2/Omi.Toxicology research · 2016Article
- Caspases shutdown nonsense-mediated mRNA decay during apoptosis.Cell death and differentiation · 2015Article
- The 5' and 3' ends of alphavirus RNAs--Non-coding is not non-functional.Virus research · 2015Review
- Article
23 more citing papers are in PubMed but not listed here.
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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Although much is known about the multiple mechanisms which induce apoptosis, comparatively little is understood concerning the execution phase of apoptosis and the mechanism(s) of cell killing. Several reports have demonstrated that cellular translation is shut off during apoptosis; however, details of the mechanism of translation inhibition are lacking. Translation initiation factor 4G (eIF4G) is a crucial protein required for binding cellular mRNA to ribosomes and is known to be cleaved as the central part of the mechanism of host translation shutoff exerted by several animal viruses. Treatment of HeLa cells with the apoptosis inducers cisplatin and etoposide resulted in cleavage of eIF4G, and the extent of its cleavage correlated with the onset and extent of observed inhibition of cellular translation. The eIF4G-specific cleavage activity could be measured in cell lysates in vitro and was inhibited by the caspase inhibitor Ac-DEVD-CHO at nanomolar concentrations. A combination of in vivo and in vitro inhibitor studies suggest the involvement of one or more caspases in the activation and execution of eIF4G cleavage. Furthermore recombinant human caspase 3 was expressed in bacteria, and when incubated with HeLa cell lysates, was shown to produce the same eIF4G cleavage products as those observed in apoptotic cells. In addition, purified caspase 3 caused cleavage of purified eIF4G, demonstrating that eIF4G could serve as a substrate for caspase 3. Taken together, these data suggest that cellular translation is specifically inhibited during apoptosis by a mechanism involving cleavage of eIF4G, an event dependent on caspase activity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.