ArticlePlant physiology2016
eIF4A RNA Helicase Associates with Cyclin-Dependent Protein Kinase A in Proliferating Cells and Is Modulated by Phosphorylation.
Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
17 citing papers in PubMed, 30 citations in OpenAlex.
- SMG7 and eIF4A constitute a homeostatic module controlling P-body condensation and function of meiotic bodies.Nature communications · 2026Article
- DEAD box RNA helicases are pervasive protein kinase interactors and activators.Genome research · 2024Article
- Oncogenic PKA signaling increases c-MYC protein expression through multiple targetable mechanisms.eLife · 2023Article
- Selective recruitment of stress-responsive mRNAs to ribosomes for translation by acetylated protein S1 during nutrient stress in Escherichia coli.Communications biology · 2022Article
- Article
- The nuclear GUCT domain-containing DEAD-box RNA helicases govern gametophytic and sporophytic development in Physcomitrium patens.Plant molecular biology · 2021Article
- Linkage mapping and QTL analysis of flowering time in faba bean.Scientific reports · 2021Article
- Genome-Wide Analysis of DEAD-box RNA Helicase Family in Wheat (Frontiers in plant science · 2021Article
- Screening of Key Proteins Affecting Floral Initiation of Saffron Under Cold Stress Using iTRAQ-Based Proteomics.Frontiers in plant science · 2021Article
- Phosphorylation Site Motifs in Plant Protein Kinases and Their Substrates.Methods in molecular biology (Clifton, N.J.) · 2021Review
- Translational gene regulation in plants: A green new deal.Wiley interdisciplinary reviews. RNA · 2020Review
- Mechanisms and Regulation of RNA Condensation in RNP Granule Formation.Trends in biochemical sciences · 2020Review
- Gene Function Rather than Reproductive Mode Drives the Evolution of RNA Helicases in Sexual and Apomictic Boechera.Genome biology and evolution · 2020Article
- The DEAD-box RNA helicase eIF4A regulates plant development and interacts with the hnRNP LIF2L1 in Physcomitrella patens.Molecular genetics and genomics : MGG · 2020Article
- The MATH-BTB Protein TaMAB2 Accumulates in Ubiquitin-Containing Foci and Interacts With the Translation Initiation Machinery inFrontiers in plant science · 2019Article
- Emerging Roles of the Nuclear Cap-Binding Complex in Abiotic Stress Responses.Plant physiology · 2018Review
- Stress granule and P-body clearance: Seeking coherence in acts of disappearance.Seminars in cell & developmental biologyReview
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 4 countries.
Funding
Abstract
Eukaryotic initiation factor 4A (eIF4A) is a highly conserved RNA-stimulated ATPase and helicase involved in the initiation of messenger RNA translation. Previously, we found that eIF4A interacts with cyclin-dependent kinase A (CDKA), the plant ortholog of mammalian CDK1. Here, we show that this interaction occurs only in proliferating cells where the two proteins coassociate with 5'-cap-binding protein complexes, eIF4F or the plant-specific eIFiso4F. CDKA phosphorylates eIF4A on a conserved threonine residue (threonine-164) within the RNA-binding motif 1b TPGR. In vivo, a phospho-null (APGR) variant of the Arabidopsis (Arabidopsis thaliana) eIF4A1 protein retains the ability to functionally complement a mutant (eif4a1) plant line lacking eIF4A1, whereas a phosphomimetic (EPGR) variant fails to complement. The phospho-null variant (APGR) rescues the slow growth rate of roots and rosettes, together with the ovule-abortion and late-flowering phenotypes. In vitro, wild-type recombinant eIF4A1 and its phospho-null variant both support translation in cell-free wheat germ extracts dependent upon eIF4A, but the phosphomimetic variant does not support translation and also was deficient in ATP hydrolysis and helicase activity. These observations suggest a mechanism whereby CDK phosphorylation has the potential to down-regulate eIF4A activity and thereby affect translation.
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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.