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Translation efficiency in the pancreatic tumor in response to ketogenic diet and targeting eIF4E phosphorylation

ABSTRACT: Translation efficiency in the pancreatic tumor in response to ketogenic diet and targeting eIF4E phosphorylation

PROVIDER: PRJNA1111414 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR29016667_1.fastq.gz	Fastqsanger.gz
	SRR29016667_2.fastq.gz	Fastqsanger.gz
	SRR29016668_1.fastq.gz	Fastqsanger.gz
	SRR29016668_2.fastq.gz	Fastqsanger.gz
	SRR29016669_1.fastq.gz	Fastqsanger.gz

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Translation efficiency in the pancreatic tumor in response to ketogenic diet and targeting eIF4E phosphorylation

Project description:To investigate the translatome in the pancreatic tumor inresponse to ketogenidc diet and the combination of ketogenic diet with an inhibitor targeting eIF4E phosphorylation. We generated pancreatic tumor xenograftmice model, treated mice with regular chow, ketogenic diet or ketogenic diet with eFT508, an inhibitor targeting eIF4E phosphorylation. Then we performed Poly-RNAseq on the tumor isolated from mice upon different treatments.

2024-08-14 | GSE267398 | GEO

Translation efficiency in the mouse liver upon 24h chow or ketogenic diet fed

Project description:To investigate the translatome in the ketogenic diet fed condition and the role of phosphoralated eIF4E in it We performed polysome sequencing on chow fed and 24h ketogenic diet fed wild type mice and chow fed eIF4E S209A/S209A mice

2024-08-14 | GSE267336 | GEO

Project description:Eukaryotic translation initiation factor 4E (eIF4E)–binding protein 1 (4E-BP1) inhibits cap-dependent translation in eukaryotes by competing with eIF4G for an interaction with eIF4E. Phos-phorylation at Ser-83 of 4E-BP1 occurs during mitosis through the activity of cyclin-dependent kinase 1 (CDK1)/cyclin B rather than through canonical mTOR kinase activity. Here, we investi-gated the interaction of eIF4E with 4E-BP1 or eIF4G during interphase and mitosis. We observed that 4E-BP1 and eIF4G bind eIF4E at similar levels during interphase and mitosis. The most highly phosphorylated mitotic 4E-BP1 isoform (δ) did not interact with eIF4E, whereas a distinct 4E-BP1 phospho-isoform, EB-γ—phosphorylated at Thr-70, Ser-83, and Ser-101—bound to eIF4E during mitosis. Two-dimensional gel electropho-retic analysis corroborated the identity of the phosphorylation marks on the eIF4E-bound 4E-BP1 isoforms and uncovered a population of phosphorylated 4E-BP1 molecules lacking Thr-37/Thr-46–priming phosphorylation. Moreover, proximity ligation assays for phospho–4E-BP1 and eIF4E revealed different in situ interactions during interphase and mitosis. The eIF4E:eIF4G interaction was not inhibited, but rather increased in mitotic cells, consistent with active translation initiation during mitosis. Phospho-defective substitution of 4E-BP1 at Ser-83 did not change global translation or individual mRNA translation profiles as measured by single-cell nascent protein synthesis and eIF4G RNA-immunoprecipitation sequencing. Mitotic 5’-terminal oligopyrimidine RNA translation was active and, unlike interphase translation, resistant to mTOR inhibition. Our findings reveal the phosphorylation profiles of 4E-BP1 isoforms and their interactions with eIF4E throughout the cell cycle and indicate that 4E-BP1 does not specifically inhibit translation initiation during mitosis.

2019-06-14 | GSE131668 | GEO

eIF4E phosphorylation promotes tumorigenesis and is associated with prostate cancer progression

Project description:Translational regulation plays a critical role in cell growth and proliferation, and its dysregulation results in cancer. Aberrant expression of the mRNA 5’cap-binding protein, eIF4E, has been implicated in cancer development and progression. eIF4E activity is promoted by phosphorylation. Here we show that “knock-in” mice in which eIF4E cannot be phosphorylated are resistant to tumorigenesis in a prostate cancer model. We identify multiple candidate genes involved in the resistance to oncogenic transformation. Importantly, phosphorylation of eIF4E is increased in hormone-refractory prostate cancer, the deadliest stage of the disease. Our results highlight eIF4E phosphorylation as a critical event in tumorigenesis. Comaparison of total RNA and polysomal RNA from mouse embryo fibroblasts derived from WT and eIF4E-KI (non phosphorylatable eIF4E) mice

2010-08-17 | E-GEOD-17451 | biostudies-arrayexpress

CERES is an eIF4E-interacting protein that forms non-canonical translation initiation complexes and modulates translation during the diel cycle in plants

Project description:Translation is a fundamental step in gene expression that regulates multiple developmental and stress responses. One key step of translation is the association between eIF4E and eIF4G. This process is regulated in different eukaryotes by proteins which bind to eIF4E and block the formation of the eIF4E/eIF4G complex. Here, we report the discovery of CERES, the first functional eIF4E regulator described in plants. CERES is a modular protein that contains a LRR domain and a canonical eIF4E binding site (4E-BS), critical for CERES interaction with eIF4E in planta. CERES/eIF4E interaction excludes eIF4G from the complex. Despite this observation, CERES promotes translation in vivo interacts with eIF4A and with eIF3 in vivo and cosediments with translation initiation complexes in sucrose gradients. Moreover, ceres mutants display a sharp increase of the 80S peak and a reduction of polysome content at specific periods of the diel cycle. Super-resolution ribosome profiling demonstrates that these mutants show a change of translation efficiency of mRNAs related to light response and glucose management. Consistently, these mutants show a hypersensitive response to glucose. These data show that CERES is a “non canonical” translation initiation factor that, through the formation of alternative translation initiation complexes, modulates translation during the light cycle in plants.

2019-12-04 | GSE124290 | GEO

Hyperactive mTOR and MNK1 phosphorylation of eIF4E confer tamoxifen resistance and estrogen independence through selective mRNA translation reprogramming

Project description:Tamoxifen resistant translational reprogramming is shown to be mediated by increased expression of eIF4E and its increased availability by hyperactive mTOR, and to require phosphorylation of eIF4E at Ser209 by increased MNK activity.

2017-12-21 | GSE107590 | GEO

eIF4E phosphorylation promotes tumorigenesis and is associated with prostate cancer progression

2010-08-17 | GSE17451 | GEO

Translation efficiency in the mouse liver upon 24h chow or ketogenic diet fed

Project description:Translation efficiency in the mouse liver upon 24h chow or ketogenic diet fed

| PRJNA1111095 | ENA

The eukaryotic translation initiation factor eIF4E regulates flowering and circadian rhythm in Arabidopsis

Project description:Translation initiation is a rate-limiting step in protein synthesis. The eukaryotic translation initiation factor 4E (eIF4E) plays an essential role in the translation initiation process. However, how eIF4E-dependent translation initiation regulates plant growth and development remains not fully understood. In this study, we have found that Arabidopsis eIF4E proteins distribute both in the nucleus and cytoplasm, and only cytoplasmic eIF4E is implicated in the control of flowering time. Results of profiling the genome-wide translation by Ribo-tag sequencing further reveal that eIF4E may regulate plant flowering by affecting homeostatic translation of flowering-time genes, including the Central Oscillator Genes (COGs). Consistent with the hypothesis that transcription-translation feedback loop is the core mechanism to drive the oscillation of circadian clock, we show that the eIF4E-dependent translation modulates the rhythmic oscillation of protein abundance of the clock-related genes (CCGs). Together, our study provides mechanistic insights into how the protein translation regulates multiple developmental processed in Arabidopsis including circadian clock and photoperiodic flowering.

2023-10-25 | GSE245858 | GEO

The eukaryotic translation initiation factor eIF4E elevates steady-state m7G capping of coding and noncoding transcripts

Project description:Methyl-7-guanosine (m7G) “capping” of coding and some noncoding RNAs is critical for their maturation and subsequent activity. Here, we discovered that eukaryotic translation initiation factor 4E(eIF4E), itself a cap-binding protein, drives the expression of the capping machinery and the increased capping efficiency of ∼100 coding and noncoding RNAs. This dataset collects transcriptomic data for quantitative cap immunoprecipitation (CapIP) assay in eIF4E-Flag or vector stable U2Os cells.

2020-09-30 | GSE158728 | GEO

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