Eukaryotic translation initiation factor 4E type 3 - eIF4E type 3; eIF-4E type 3; mRNA cap-binding protein type 3; Eukaryotic translation initiation factor 4E-like 3; Eukaryotic translation initiation
- Known as:
- Eukaryotic translation initiation factor 4E classification 3 - eIF4E classification 3; eIF-4E classification 3; mRNA cap-binding protein classification 3; Eukaryotic translation initiation factor 4E-like 3; Eukaryotic translation initiation
- Catalog number:
- 10-288-22403F
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- GenWay
- Gene target:
- Eukaryotic translation initiation factor 4E type 3 - eIF4E 3; eIF-4E mRNA cap-binding protein 4E-like
Related genes to: Eukaryotic translation initiation factor 4E type 3 - eIF4E type 3; eIF-4E type 3; mRNA cap-binding protein type 3; Eukaryotic translation initiation factor 4E-like 3; Eukaryotic translation initiation
- Gene:
- EIF4E NIH gene
- Name:
- eukaryotic translation initiation factor 4E
- Previous symbol:
- EIF4EL1, EIF4F
- Synonyms:
- EIF4E1
- Chromosome:
- 4q23
- Locus Type:
- gene with protein product
- Date approved:
- 1991-07-09
- Date modifiied:
- 2015-08-25
Related products to: Eukaryotic translation initiation factor 4E type 3 - eIF4E type 3; eIF-4E type 3; mRNA cap-binding protein type 3; Eukaryotic translation initiation factor 4E-like 3; Eukaryotic translation initiation
Related articles to: Eukaryotic translation initiation factor 4E type 3 - eIF4E type 3; eIF-4E type 3; mRNA cap-binding protein type 3; Eukaryotic translation initiation factor 4E-like 3; Eukaryotic translation initiation
- The best-characterized functional motifs of the potyviral Helper-Component protease (HC-Pro) responding for aphid transmission, RNA silencing suppression, movement, symptom development, and replication are gathered in this review. The potential cellular protein targets of plant virus proteases remain largely unknown despite their multifunctionality. The HC-Pro catalytic domain, as a cysteine protease, autoproteolytically cleaves the potyviral polyproteins in the sequence motif YXVG/G and is not expected to act on host targets; however, 146 plant proteins in the clade containing this motif were searched in the UniProtKB database and are discussed. On the other hand, more than 20 interactions within the entire HC-Pro structure are known. Most of these interactions with host targets (such as the 20S proteasome, methyltransferase, transcription factor eIF4E, and microtubule-associated protein HIP2) modulate the cellular environments for the benefit of virus accumulation or contribute to symptom severity (interactions with MinD, Rubisco, ferredoxin) or participate in the suppression of RNA silencing (host protein VARICOSE, calmodulin-like protein). On the contrary, the interaction of HC-Pro with triacylglycerol lipase, calreticulin, and violaxanthin deepoxidase seems to be beneficial for the host plant. The strength of these interactions between HC-Pro and the corresponding host protein vary with the plant species. Therefore, these interactions may explain the species-specific sensitivity to potyviruses. - Source: PubMed
Publication date: 2024/04/29
Hýsková VeronikaBělonožníková KateřinaChmelík JosefHoffmeisterová HanaČeřovská NoemiMoravec TomášRyšlavá Helena - Helicobacter pylori (H. pylori) infection is the main risk factor for gastric cancer. The SRY-Box Transcription Factor 9 (SOX9) serves as a marker of stomach stem cells. We detected strong associations between AURKA and SOX9 expression levels in gastric cancers. Utilizing in vitro and in vivo mouse models, we demonstrated that H. pylori infection induced elevated levels of both AURKA and SOX9 proteins. Notably, the SOX9 protein and transcription activity levels were dependent on AURKA expression. AURKA knockdown led to a reduction in the number and size of gastric gland organoids. Conditional knockout of AURKA in mice resulted in a decrease in SOX9 baseline level in AURKA-knockout gastric glands, accompanied by diminished SOX9 induction following H. pylori infection. We found an AURKA-dependent increase in EIF4E and cap-dependent translation with an AURKA-EIF4E-dependent increase in SOX9 polysomal RNA levels. Immunoprecipitation assays demonstrated binding of AURKA to EIF4E with a decrease in EIF4E ubiquitination. Immunohistochemistry analysis on tissue arrays revealed moderate to strong immunostaining of AURKA and SOX9 with a significant correlation in gastric cancer tissues. These findings elucidate the mechanistic role of AURKA in regulating SOX9 levels via cap-dependent translation in response to H. pylori infection in gastric tumorigenesis. - Source: PubMed
Publication date: 2024/05/08
Gomaa AhmedMaacha SelmaPeng DunfaSoutto MohammedGenoula MelanieBhat NadeemCao LonglongZhu ShouminCastells AntoniChen ZhibinZaika AlexanderMcDonald Oliver GEl-Rifai Wael - Activation of brown adipose tissue (BAT) thermogenesis increases energy expenditure and alleviates obesity. Here we discover that histone methyltransferase suppressor of variegation 4-20 homolog 2 (Suv420h2) expression parallels that of Ucp1 in brown and beige adipocytes and that Suv420h2 knockdown significantly reduces, whereas Suv420h2 overexpression significantly increases Ucp1 levels in brown adipocytes. Suv420h2 knockout (H2KO) mice exhibit impaired cold-induced thermogenesis and are prone to diet-induced obesity. In contrast, mice with specific overexpression of Suv420h2 in adipocytes display enhanced cold-induced thermogenesis and are resistant to diet-induced obesity. Further study shows that Suv420h2 catalyzes H4K20 trimethylation at eukaryotic translation initiation factor 4E-binding protein 1 (4e-bp1) promoter, leading to down-regulated expression of 4e-bp1, a negative regulator of the translation initiation complex. This in turn up-regulates PGC1α protein levels, which is associated with increased expression of thermogenic program. We conclude that Suv420h2 is a key regulator of brown/beige adipocyte development and thermogenesis. - Source: PubMed
Publication date: 2024/05/07
Cui XinCao QiangLi FenfenJing JiaLiu ZhixueYang XiaosongSchwartz Gary JYu LiqingShi HuidongShi HangXue Bingzhong - The phosphorylation of eukaryotic translational initiation factors has been shown to play a significant role in controlling the synthesis of protein. Viral infection, environmental stress, and growth circumstances cause phosphorylation or dephosphorylation of plant initiation factors. Our findings indicate that casein kinase 2 can phosphorylate recombinant wheat eIFiso4E and eIFiso4G generated from E. coli in vitro. For wheat eIFiso4E, Ser-207 was found to be the in vitro phosphorylation site. eIFiso4E lacks an amino acid that can be phosphorylated at the position corresponding to Ser-209, the phosphorylation site in mammalian eIF4E, yet phosphorylation of eIFiso4E has effects on VPg binding affinity that are similar to those of phosphorylation of mammalian eIF4E. The addition of VPg and phosphorylated eIFiso4F to depleted wheat germ extract (WGE) leads to enhancement of translation of both uncapped and capped viral mRNA. The addition of PABP together with eIFiso4Fp and eIF4B to depleted WGE increases both uncapped and capped mRNA translation. However, it exhibits a translational advantage specifically for uncapped mRNA, implying that the phosphorylation of eIFiso4F hinders cap binding while promoting VPg binding, thereby facilitating uncapped translation. These findings indicate TEV virus mediates VPg-dependent translation by engaging a mechanism entailing phosphorylated eIFiso4Fp and PABP. To elucidate the molecular mechanisms underlying these observed effects, we studied the impact of PABP and/or eIF4B on the binding of VPg with eIFiso4Fp. The inclusion of PABP and eIF4B with eIFiso4Fp resulted in about 2-fold increase in affinity for VPg (Kd = 24 ± 1.7 nM), as compared to the affinity of eIFiso4Fp alone (Kd = 41.0 ± 3.1 nM). The interactions between VPg and eIFiso4Fp were determined to be both enthalpically and entropically favorable, with the enthalpic contribution accounting for 76-97% of the ΔG at 25°C, indicating a substantial role of hydrogen bonding in enhancing the stability of the complex. The binding of PABP to eIFiso4Fp·4B resulted in a conformational alteration, leading to a significant enhancement in the binding affinity to VPg. These observations suggest PABP enhances the affinity between eIFiso4Fp and VPg, leading to an overall conformational change that provides a stable platform for efficient viral translation. - Source: PubMed
Publication date: 2024/05/02
Khan Mateen AYumak SumeyraMiyoshi Hiroshi - - Source: PubMed
Publication date: 2024/05/01
Huang FanGonçalves ChristopheBartish MargaritaRémy-Sarrazin JoelleIssa Mark ECordeiro BrendanGuo QianyuEmond AudreyAttias MikhaelYang WilliamPlourde DanySu JieGimeno Marina GodoyZhan YaoGalán AlbaRzymski TomaszMazan MilenaMasiejczyk MagdalenaFaber JacekKhoury ElieBenoit AlexandreGagnon NataschaDankort DavidJourne FabriceGhanem Ghanem EKrawczyk Connie MSaragovi H UriPiccirillo Ciriaco ASonenberg NahumTopisirovic IvanRudd Christopher EMiller Wilson HDel Rincón Sonia V