mRNAs containing extensive secondary structure in their 5′ non‐coding region translate efficiently in cells overexpressing initiation factor eIF‐4E.
Explore this paper's citation graph
Summary
It is reported that overexpression of eIF‐4E facilitates the translation of mRNAs containing excessive secondary structure in their 5′ non‐coding region, which may represent one mechanism by which eIF-4E regulates cell growth and transforms cells in culture.
- Type
- article
- Published
- 1992-11-01
- Cited by
- 436
- References
- 54
- Access
- Open access
- OpenAlex
- https://openalex.org/W67546116
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:45776498
Keywords
Library science, Biology, Computer science
References
- Capping of eucaryotic mRNAs.
- Translation initiation factors induce DNA synthesis and transform NIH 3T3 cells.
- Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F
- New initiation factor activity required for globin mRNA translation.
- Differential stimulation of phosphorylation of initiation factors eIF-4F, eIF-4B, eIF-3, and ribosomal protein S6 by insulin and phorbol esters.
- Two forms of purified m7G-cap binding protein with different effects on capped mRNA translation in extracts of uninfected and poliovirus-infected HeLa cells.
- Phosphorylation site of eukaryotic initiation factor 4E.
- Involvement of eukaryotic initiation factor 4A in the cap recognition process.
- Simultaneous cytoplasmic redistribution of ribosomal protein L32 mRNA and phosphorylation of eukaryotic initiation factor 4E after mitogenic stimulation of Swiss 3T3 cells.
- Heat shock impairs the interaction of cap-binding protein complex with 5' mRNA cap.
- Regulated phosphorylation and low abundance of HeLa cell initiation factor eIF-4F suggest a role in translational control. Heat shock effects on eIF-4F.
- Phorbol esters stimulate phosphorylation of eukaryotic initiation factors 3, 4B, and 4F.
- Immunological detection of the messenger RNA cap-binding protein.
- Protein phosphorylation controls translation rates.
- Structural requirements for trans activation of human immunodeficiency virus type 1 long terminal repeat-directed gene expression by tat: importance of base pairing, loop sequence, and bulges in the tat-responsive sequence
- Alteration of the major phosphorylation site of eukaryotic protein synthesis initiation factor 4E prevents its association with the 48 S initiation complex.
- ATP-dependent unwinding of messenger RNA structure by eukaryotic initiation factors.
- Insulin induction of ornithine decarboxylase. Importance of mRNA secondary structure and phosphorylation of eucaryotic initiation factors eIF-4B and eIF-4E.
- Cap binding protein complex that restores protein synthesis in heat-shocked Ehrlich cell lysates contains highly phosphorylated eIF-4E.
- Involvement of the 24-kDa cap-binding protein in regulation of protein synthesis in mitosis.
Cited by
- Characterization of the in Vivo Phosphorylation Sites of the mRNA·Cap-binding Complex Proteins Eukaryotic Initiation Factor-4E and p20 in Saccharomyces cerevisiae(*)
- Control of PHAS-I by Insulin in 3T3-L1 Adipocytes
- Heat Shock Increases the Association of Binding Protein-1 with Initiation Factor 4E*
- Translational control in vertebrate development.
- Oral leucine administration stimulates protein synthesis in rat skeletal muscle.
- Igbp1 is part of a positive feedback loop in stem cell factor-dependent, selective mRNA translation initiation inhibiting erythroid differentiation.
- Differential contribution of the m7G-cap to the 5′ end-dependent translation initiation of mammalian mRNAs
- Identification of Cardiac Glycoside Molecules as Inhibitors of c-Myc IRES-Mediated Translation
- Role of the eIF4E binding protein 4E‐BP1 in regulation of the sensitivity of human pancreatic cancer cells to TRAIL and celastrol‐induced apoptosis
- Temporal and spatial regulation of translation in the mammalian oocyte via the mTOR–eIF4F pathway
- MYC: connecting selective transcriptional control to global RNA production
- Cap-dependent and cap-independent translation: operational distinctions and mechanistic interpretations.
- mTOR signaling to translation.
- Phosphorylation of mammalian eIF4E by Mnk1 and Mnk2: tantalizing prospects for a role in translation.
- Regulation of translation elongation factor‐2 by insulin via a rapamycin‐sensitive signalling pathway.
- The regulation of eIF4F during cell growth and cell death.
- Deregulation of cell growth and malignant transformation.
- DENDRITIC CELLS, RAPAMYCIN AND TRANSPLANT TOLERANCE
- Etude par génétique inverse du gène codant la protéine TARGET OF RAPAMYCIN d'Arabidopsis thaliana (AtTOR), l'homologue d'une kinase contrôlant la croissance cellulaire chez les eucaryotes
- Cap-Independent Translation
Related papers
- Cloning and Characterization of Rat BAT3 cDNA
- HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-mediated acetylation of p53.
- Anthoxanthum Mosaic Virus
- Ecological and evolutionary importance of neighbors in the grass Anthoxanthum odoratum
- Memoirs: The Structure and Biology of Schizoneura Lanigera, Hausmann or Woolly Aphis of the Apple Tree: Part I.--The Apterous Viviparous Female
- HSV-1 strain McKrae is more neuroinvasive than HSV-1 KOS after corneal or vaginal inoculation in mice
- Bat3 deficiency accelerates the degradation of Hsp70-2/HspA2 during spermatogenesis
- Viral Pathogens and the Advantage of Sex in the Perennial Grass Anthoxanthum odoratum [and Discussion]
- Biology of Ecologically Marginal Populations of Anthoxanthum odoratum. I. Phenetics and Dynamics
- Pan-genome study of Thermococcales reveals extensive genetic diversity and genetic evidence of thermophilic adaption.