ArticleProceedings of the National Academy of Sciences of the United States of America2015
Protein synthesis during cellular quiescence is inhibited by phosphorylation of a translational elongation factor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
48 citing papers in PubMed, 69 citations in OpenAlex.
- The alarmone pGpp inhibits translation through GTP depletion.Nucleic acids research · 2026Article
- Dry versus wet dormancy: suspended lives ofmSystems · 2026Review
- Hydroxyl radical footprinting modification reveals an intradomain communication pathway in EFL1 disrupted by a Shwachman-Diamond syndrome-associated mutation.Protein science : a publication of the Protein Society · 2026Article
- TUFM: a central regulator in mitochondrial quality control and beyond.Cell death discovery · 2026Review
- Capturing ribosomal structures in cellular extracts with cryoPRISM: A purification-free cryoEM approach reveals novel structural states.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Starvation-independent alarmone production inhibits translation through GTP depletion.bioRxiv : the preprint server for biology · 2026Article
- Lysine acetylome profiling reveals a dual regulatory role in carbon flux redirection and RNA degradation inhibition inFrontiers in microbiology · 2026Article
- Reversible proliferative arrest induced by rapid depletion of RNase MRP.Nature communications · 2025Article
- KAT5 regulates neurodevelopmental states associated with G0-like populations in glioblastoma.Nature communications · 2025Article
- Stage-specific MCM protein expression inFrontiers in cellular and infection microbiology · 2025Article
- Article
- Translation in Bacillus subtilis is spatially and temporally coordinated during sporulation.Nature communications · 2024Article
- Dynamic Protein Phosphorylation inMicroorganisms · 2024Article
- YfmR is a translation factor that prevents ribosome stalling and cell death in the absence of EF-P.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Loratadine Combats Methicillin-ResistantACS infectious diseases · 2024Article
- Rippling life on a dormant planet: hibernation of ribosomes, RNA polymerases, and other essential enzymes.Frontiers in microbiology · 2024Review
- YfmR is a translation factor that prevents ribosome stalling and cell death in the absence of EF-P.bioRxiv : the preprint server for biology · 2023Article
- Giving a signal: how protein phosphorylation helps Bacillus navigate through different life stages.FEMS microbiology reviews · 2023Review
- Quiescence ofMicroorganisms · 2023Article
- Calcium lignosulfonate modulates physiological and biochemical responses to enhance shoot multiplication inPhysiology and molecular biology of plants : an international journal of functional plant biology · 2023Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In nature, most organisms experience conditions that are suboptimal for growth. To survive, cells must fine-tune energy-demanding metabolic processes in response to nutrient availability. Here, we describe a novel mechanism by which protein synthesis in starved cells is down-regulated by phosphorylation of the universally conserved elongation factor Tu (EF-Tu). Phosphorylation impairs the essential GTPase activity of EF-Tu, thereby preventing its release from the ribosome. As a consequence, phosphorylated EF-Tu has a dominant-negative effect in elongation, resulting in the overall inhibition of protein synthesis. Importantly, this mechanism allows a quick and robust regulation of one of the most abundant cellular proteins. Given that the threonine that serves as the primary site of phosphorylation is conserved in all translational GTPases from bacteria to humans, this mechanism may have important implications for growth-rate control in phylogenetically diverse organisms.
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Registered trials
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.