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Human EIF4EBP1 Protein expressed in Escherichia coli (E. coli) - ABIN2001934
Hara, Maruki, Long, Yoshino, Oshiro, Hidayat, Tokunaga, Avruch, Yonezawa: Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action. in Cell 2002
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Ovarian tumors with p-mTOR, p-4EBP1 and p-P70S6K protein expressions were investigated in a Cox model that was also adjusted for FIGO stage. High p-4EBP1 was independently associated with poor overall survival (OS). When the three proteins are combined, high p-4EBP1 was independently associated with a poor OS and showed a borderline association with poor progression-free survival.
Study demonstrated key roles for 4E-BP1 and 4E-BP2 during tumor development and during tumor hypoxia. These factors maintain an ability to slow tumor progression in prostate cancer in the face of constitutive mTOR activation arising from loss of PTEN, and are also important in promoting survival of hypoxic cells once cancer has developed.
High-expressions of mTOR and 4E-BP1 in patients with extranodal Nasal-type NK/T-cell Lymphoma (ENKTCL) are related to the biological progression and recurrence of ENKTCL
Data have shown that the activation level of the 4EBP1/eIF4E axis in localized clear cell renal carcinoma (ccRCC) can contribute, not only to tumor recurrence, but also to the timing of the recurrence after curative nephrectomy. This activation can affect early and late recurrence events differently.
The phosphorylation dynamics and rapamycin sensitivity of 4E-BP1 and S6K1 are regulated independently.
high p-4E-BP1 level is associated with tumor progression and adverse prognosis in colorectal cancer
Rapamycin-insensitive mTORC1 signaling via 4E-BP1 is a critical pathway for TGF-beta1 stimulated collagen synthesis in human lung fibroblasts, whereas canonical PI3K/Akt signaling is not required.
L-type amino acid transporter 1 (LAT1) inhibitor, BCH reduces the phosphorylation of mechanistic target of rapamycin kinase (mTOR) downstream target eukaryotic translation initiation factor 4E binding protein 1 (4EBP1) in fibroblast-like synoviocytes from patients with rheumatoid arthritis. Silencing eIF4E neutralized the stimulation of interleukin-17 on LAT1.
Using an mTORspecific signalling pathway phospho array we revealed that NVPBEZ235 significantly decreased phosphorylation of 4EBP1 (Thr70), the downstream target of mTORC1.
These results demonstrate a previously unrecognized role of IL24 in inhibition of translation, mediated through both phosphorylation of eIF2alpha and dephosphorylation of 4E-BP1, and provide the first direct evidence for translation control of gene-specific expression by IL24
High p-4E-BP1 expression was significantly associated with lymphovascular invasion (LVI) (p=0.003), perineural invasion (PNI) (p=0.001), tumor stage (p=0.024), nodal stage (p=0.000), metastatic status (p=0.027), and disease stage (p=0.001).
Numerous protein kinases can be responsible for mTOR independent 4E-BP1 phosphorylation in cancer. (Review)
PI3K kinase activity is necessary for maintaining 4E-BP1 stability. Our results also suggest 4E-BP1 a novel biological role of regulating cell cycle G2 checkpoint in responding to IR stress in association with controlling CHK2 phosphorylation
Findings suggest that mitotic CDK1-directed phosphorylation of delta-4E-BP1 may yield a gain of function, distinct from translation regulation, that may be important in tumorigenesis and mitotic centrosome function.
p4EBP1 was independently predictive for pathologic complete response in PIK3CA wild-type tumors.
Data show that 4EGI-1 compound induced apoptosis in nasopharyngeal carcinoma cells through the death receptor 5 (DR5) on 4E-BP1 dephosphorylation exerting positive influence on their anti-tumor activities.
p4EBP1 overexpression was predominant in patients with metastasis to the regional lymph nodes in colorectal cancer. Moderate/high expression of p4EBP1 protein was significantly associated with adverse overall survival (OS) in patients.
There were significantly higher expressions of p-eIF4E and p-4EBP-1 proteins in the cases with lymph node metastasis than in those without lymph node metastasis.
4E-BP1 has tumor suppressor activity by inhibiting eIF4E and, thus, blocking mRNA translation and proliferation. This is corroborated by elevated levels of phosphorylated and hence inactive 4E-BP1, which are detected in various cancers
Rotterlin inhibits mTORC1 and 4EBP1 activity in melanoma cells, inhibiting protein synthesis and promoting cell death.
Intracellular osteopontin can regulate GSK3beta and 4EBP1 phosphorylation to inhibit TLR4-mediated inflammatory responses.
Genetic deletion of 4E-BP1/2 in macrophages increased endogenous IL-10.
4E-BP proteins may prevent excess lipid accumulation in skeletal muscle and suggest that 4E-BPs are key regulators of muscle homeostasis regardless of insulin sensitivity.
our results show that the phosphorylation of 4E-BP1 promotes translation at the onset of meiosis to support the spindle assembly and suggest an important role of CDK1 and mTOR kinases in this process
Lack of Def6 results in deregulation of Bcl6 protein synthesis in T cells as a result of enhanced activation of the mTORC1-4E-BP-eIF4E axis.
decreasing cap-dependent translation by expressing a constitutively active mutant of the translational repressor eukaryotic initiation factor 4E-binding protein 1 (4E-BP1) prevents neuronal misplacement and soma enlargement, while partially rescuing dendritic hypertrophy induced by hyperactive mTORC1.
we show that simultaneous inhibition of mTOR signaling to both S6K1 and 4E-BP1 is sufficient to reduce AKT-induced muscle growth and render it insensitive to the mTORC1-inhibitor rapamycin
4E-BP1 is a gender-specific suppressor of obesity that regulates insulin sensitivity and energy metabolism.
The authors now show that West Nile virus growth and protein expression are dependent on mTORC1 mediated-regulation of the eukaryotic translation initiation factor 4E-binding protein/eukaryotic translation initiation factor 4E-binding protein (4EBP/eIF4E) interaction and eukaryotic initiation factor 4F (eIF4F) complex formation to support viral growth and viral protein expression.
p-mTOR, p-4EBP1, HIF-1alpha and VEGF together are involved in the pathogenesis of asthma.
Thus, translational control by 4E-BP1 downstream of mTOR effects the expression of neuroligin 1 and excitatory synaptic transmission in the spinal cord, and thereby contributes to enhanced mechanical nociception.
The findings support a model whereby elevated 4E-BP1 expression observed in the retina of diabetic rodents is the result of O-GlcNAcylation of 4E-BP1 within its PEST motif.
The mTORC1 effectors S6K1 and 4E-BP play different roles in CNS axon regeneration.
Oxidative stress-induced premature senescence occurred due to impaired autophagy function through 4EBP1 phosphorylation.
Data show that deletion of eukaryotic translation initiation factor 4E-binding protein 1/2 (4E-BP1/2) in erythroid cells rendered them resistant to mammalian target of rapamycin complex 1 (TORC1) inhibition and restored hemoglobin production.
Rotenone induction of hydrogen peroxide inhibits mTOR-mediated S6K1 and 4E-BP1/eIF4E pathways, resulting in caspase-dependent and -independent apoptosis in neuronal cells.
These findings indicate that regulation of 4E-BP1 in skeletal muscle may serve as an important conduit through which mTORC1 controls metabolism.
Disruption of genes encoding Eif4ebp1 and Eif4ebp2 does not alter basal or sepsis-induced changes in skeletal muscle protein synthesis in male or female mice.
4E-BP1/2-null cells express less ATGL and accumulate more fat than control cells, while knock down of Egr1 in 4E-BP1/2-null cells increases ATGL expression and decreases fat storage.
mTORC1 also regulates HIF-1alpha synthesis on a translational level via co-operative regulation of both initiation factor 4E-binding protein 1 (4E-BP1) and ribosomal protein S6 kinase-1 (S6K1)
4E-BP determines lifespan in the context of temperature changes, revealing a genetic mechanism for cold-induced longevity in this model organism. Our results suggest that the 4E-BP pathway, chiefly thought of as a nutrient sensor, may represent a master metabolic switch responding to diverse environmental factors
Here, the authors show that cell autonomous insulin signaling within the Drosophila CM9 motor neuron regulates the release of neurotransmitter via alteration of the synaptic vesicle fusion machinery. This effect of insulin utilizes the FOXO-dependent regulation of the thor gene, which encodes the Drosophila homologue of the eif-4e binding protein (4eBP).
GCN2 and ATF4 are important regulators of 4E-BP transcription during normal drosophila development and aging.
longevity assurance mutants of chico, the Drosophila insulin receptor substrate homolog, require Drosophila d4eBP to slow aging.
These results indicate that the Ccr4-Not complex controls expression of 4E-BP at multiple levels and adjusts the magnitude of the total effect.
eIF4E-binding protein requires non-canonical 4E-binding motifs and a lateral surface of eIF4E to repress translation.
PcG proteins can directly modulate cell growth in Drosophila, in part by regulating Thor expression
These findings reveal an organism-wide regulation of proteostasis in response to muscle aging and a key role of FOXO/4E-BP signaling in the coordination of organismal and tissue aging.
Induction of 4EBP likely leads to growth inhibition by Dfoxo, whereas activation of InR provides a novel transcriptionally induced feedback control mechanism.
S6 kinase (dS6K) and a single 4E-BP (d4E-BP) are phosphorylated via the insulin and target of rapamycin (TOR) signaling pathways.
Drosophila 4E-BP activity becomes critical for survival under dietary restriction and oxidative stress, and is linked to life span.
Analysis of Drosophila 4E-BP(null) mutant survival upon infection with C. albicans showed that 4E-BP plays an important role in host defense.
Results show that it is via 4E-BP, regulators of the translation factor eIF4E, FOXO and TOR also converge to regulate protein synthesis.
chronic inactivation of 4E-BP by LRRK2 with pathogenic mutations deregulates protein translation, eventually resulting in age-dependent loss of DA neurons
4eBP is sufficient to protect long-term cardiac function against age-related decline in Drosophila.
The translational repressor 4E-BP, the eukaryotic translation initiation factor 4E binding protein, was upregulated upon dietary restriction and mediated dietary restriction dependent changes in mitochondrial activity and lifespan extension.
This translational inhibitor is an effector of PI(3)K/Akt signalling and cell growth in Drosophila.
Arg, Leu, and Gln act coordinately to stimulate proliferation of pTr cells through activation of the MTOR-RPS6K-RPS6-EIF4EBP1 signal transduction pathway.
This gene encodes one member of a family of translation repressor proteins. The protein directly interacts with eukaryotic translation initiation factor 4E (eIF4E), which is a limiting component of the multisubunit complex that recruits 40S ribosomal subunits to the 5' end of mRNAs. Interaction of this protein with eIF4E inhibits complex assembly and represses translation. This protein is phosphorylated in response to various signals including UV irradiation and insulin signaling, resulting in its dissociation from eIF4E and activation of mRNA translation.
eIF4E-binding protein 1
, eukaryotic translation initiation factor 4E-binding protein 1
, phosphorylated heat- and acid-stable protein regulated by insulin 1
, Eif4e-binding protein
, eIF-4E-binding protein
, eif4e-binding protein 4EBP
, eukaryotic initiation factor 4E binding protein
, eukaryotic initiation factor 4E-binding protein
, eukaryotic translation initiation factor 4E binding protein
, eukaryotic translation initiation factor 4E-binding protein
, insulin-stimulated eIF-4E binding protein
, lethal (2) 06270
, eukaryotic translation initiation factor 4E binding protein 1
, translation initiation factor 4E binding protein 1