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RIO kinase 3 (RIOK3 (Montrer RIOK3 Protéines)) positively regulates the activity of the AKT/mTOR (Montrer FRAP1 Protéines) pathway in glioma cells.
High AKT1 phosphorylation is associated with colorectal carcinoma.
Results show that AKT1 was associated with hypertension in Mexican Mestizos but not Mexican Amerindians.
TERT (Montrer TERT Protéines) could induce thyroid carcinoma cell proliferation mainly through the PTEN/AKT signaling pathway.
findings uncover a new function of p53 (Montrer TP53 Protéines) in the regulation of Akt signaling and reveal how p53 (Montrer TP53 Protéines), ASS1 (Montrer ASS1 Protéines), and Akt are interrelated to each other.
We performed quantitative mass spectrometry of IAV1918-infected cells to measure host protein dysregulation. Selected proteins were validated by immunoblotting and phosphorylation levels of members of the PI3K (Montrer PIK3CA Protéines)/AKT/mTOR (Montrer FRAP1 Protéines) pathway were assessed.
Radiation resistance tumors have upregulated Onzin and POU5F1 (Montrer POU5F1 Protéines) expression.
The essential role of AKT in the endocrine therapy resistance in estrogen receptor (Montrer ESR1 Protéines)-positive, HER2 (Montrer ERBB2 Protéines)-negative breast cancer.[review]
FAL1 may work as a ceRNA to modulate AKT1 expression via competitively binding to miR (Montrer MLXIP Protéines)-637 in HSCR (Montrer EDNRB Protéines).
The overexpression of CHIP significantly increased the migration and invasion of the DU145 cells, which is possible due to activation of the AKT signaling pathway and upregulation of vimentin (Montrer VIM Protéines). The expression level of CHIP was observed to be increased in human prostate cancer tissues compared with the adjacent normal tissue.
M-CSF (Montrer CSF1R Protéines)-evoked ERK1/2 activation was decreased, whereas AKT activation was enhanced in SHP2 (Montrer PTPN11 Protéines)-deficient BMMs. ERK1/2, via its downstream target RSK2 (Montrer RPS6KA3 Protéines), mediates this negative feedback by negatively regulating phosphorylation of M-CSF (Montrer CSF1R Protéines) receptor at Tyr721 and, consequently, its binding to p85 (Montrer ECM1 Protéines) subunit of PI3K and PI3K activation.
Site-directed mutagenesis of Akt at Cys224 revealed that S-nitrosylation at this site was pivotal for the reduced phosphorylation at Akt Ser473, which led to impaired Akt signaling. Furthermore, on HHcy challenge, as compared with GSNOR (Montrer ADH5 Protéines)(+/+)ApoE (Montrer APOE Protéines)(-/-) littermate controls, GSNOR (Montrer ADH5 Protéines)(-/-)ApoE (Montrer APOE Protéines)(-/-) double knockout mice showed reduced T-cell activation with concurrent reduction of atherosclerosis.
the present study suggested that Pulsed electromagnetic fields (PEMFs) reduced osteoclast formation from RAW264.7 macrophages via inhibition of the Akt/mTOR (Montrer FRAP1 Protéines) signaling pathway. These findings provided novel insight into the mechanisms through which PEMFs suppress osteoclast differentiation.
Here, we describe a role for PI3K/AKT in the regulation of TRF1 (Montrer TERF1 Protéines), an essential component of the shelterin complex. PI3K and AKT chemical inhibitors reduce TRF1 (Montrer TERF1 Protéines) telomeric foci and lead to increased telomeric DNA damage and fragility. TRF1 (Montrer TERF1 Protéines) is phosphorylated by AKT regulating TRF1 (Montrer TERF1 Protéines) protein stability and TRF1 (Montrer TERF1 Protéines) binding to telomeric DNA in vitro and are important for in vivo TRF1 (Montrer TERF1 Protéines) telomere location and cell viability.
High AKT1 expression is associated with cardiac hypertrophy.
CTRP1 protected against Dox-induced cardiotoxicity via activation of AKT
Noise exposure led to enhanced JNK (Montrer MAPK8 Protéines) phosphorylation and IRS1 (Montrer IRS1 Protéines) serine phosphorylation as well as reduced Akt phosphorylation in skeletal muscles in response to exogenous insulin (Montrer INS Protéines) stimulation.
WT PDCD5 (Montrer PDCD5 Protéines) competitively inhibited interaction between histone deacetylase 3 (HDAC3 (Montrer HDAC3 Protéines)) and AKT, but PDCD5 (Montrer PDCD5 Protéines)(L6R), an HDAC3 (Montrer HDAC3 Protéines)-binding-deficient mutant, did not. Knockdown of PDCD5 (Montrer PDCD5 Protéines) accelerated HDAC3 (Montrer HDAC3 Protéines)-AKT interaction, AKT and eNOS (Montrer NOS3 Protéines) phosphorylation, and nitric oxide (NO) production
both NAD and NADH significantly increased the intracellular ATP levels of BV2 microglia, which were attenuated by SIRT2 siRNA, the SIRT2 inhibitor AGK2, and the phosphatidylinositol 3-kinase/Akt inhibitor LY294002. Results suggested that SIRT2 mediates the NAD-induced and NADH-induced increase in Akt phosphorylation in BV2 microglia.
The metabolic defects of cycG (Montrer CCNG1 Protéines) mutant animals are abrogated by a concomitant loss of Wdb, CycG (Montrer CCNG1 Protéines) presumably influences Akt1 activity at the PP2A (Montrer PPP2R2B Protéines) nexus; Well rounded (Wrd), another B' subunit of PP2A (Montrer PPP2R2B Protéines) in Drosophila, binds CycG (Montrer CCNG1 Protéines) similar to Wdb, and that its loss ameliorates some, but not all, of the metabolic defects of cycG (Montrer CCNG1 Protéines) mutants.
Our findings demonstrated that lovastatin restored LRRK2-G2019S neurite degeneration by augmenting Akt/NRF2 pathway and inhibiting downstream GSK3b activity, which decreased phospho-tau levels. We suggested that lovastatin is a potential disease-modifying agent for LRRK2-G2019S parkinsonism.
subtle manipulation of foxo through Akt1 can enhance survival during adverse nutrient conditions in Drosophila.
The developmental delay of these novel Akt1 hypomorphs results in a latent phenotype uncovered by generation of somatic clones
these data show that Drosophila Trbl has a conserved role to bind Akt and block Akt-mediated insulin signaling, and implicate Trib proteins as novel sites of signaling pathway integration that link nutrient availability with cell growth and proliferation
AKT1 and caspase-dependent regulation of Acn stability adjusts basal autophagy levels.
Akt1 governs two critical elements of synapse development, neurotransmitter receptor (Montrer GRIN1 Protéines) localization, and postsynaptic membrane elaboration
Tsc2 mutants showed a dramatic decrease in the levels of phosphorylated Akt, and interestingly, Akt mutants phenocopied Tsc2 mutants, leading to the hypothesis that Tsc2 and Akt might work via the same genetic pathway to regulate synapse growth.
Hippo signaling not only blocks cell division and promotes apoptosis, but also regulates cellular growth by inhibiting the Akt pathway activity.
Regeneration of Drosophila sensory neuron axons and dendrites is regulated by the Akt pathway involving Pten and microRNA bantam.
Thus, activation of STAT3 (Montrer STAT3 Protéines) and inactivation of AKT signaling are involved in structural regression of the corpus luteum.
the measurement of levels of PI3K-Akt pathway components in FCs from ovarian follicles carrying oocytes with distinct developmental competences is a useful tool to identify putative molecular pathways involved in the acquisition of oocyte competence.
These results demonstrate that activation of AKT is required for gonadotropin regulation of CTNNB1 (Montrer CTNNB1 Protéines) accumulation and subsequent ovarian E2 production.
Caveolin-1 (Montrer CAV1 Protéines) scaffolding domain residue phenylalanine 92 modulates Akt signaling
TG2 (Montrer TGM2 Protéines) contributes to 5-hydroxytryptamine-induced distal pulmonary artery smooth muscle cell proliferation via promotion of AKT signaling, likely via its serotonylation.
results suggest that PI3K-Akt activity is important for the internalization of S. aureus and phosphorylation of GSK-3alpha, GSK-3beta, and NF-kappaB (Montrer NFKB1 Protéines).
The current study was designed to determine mechanisms underlying 20-hydroxyeicosatetraenoic acid -stimulated nitric oxide (NO) release, and particularly the role of NADPH oxidase (Montrer NOX1 Protéines), reactive oxygen species, and PI3-kinase (Montrer PIK3CA Protéines) in stimulated NO release.
PI3K/Akt and p53 (Montrer TP53 Protéines) are redox-regulated in bovine aortic endothelial cells exposed to hydrogen peroxide
Thus our data demonstrate that hypoxia-induced adventitial fibroblast proliferation requires activation and interaction of PI3K, Akt, mTOR, p70S6K, and ERK1/2.
Gab1 tyrosine phosphorylation is stimulated by flow shear stress to mediate protein kinase B and endothelial nitric-oxide synthase (Montrer NOS3 Protéines) activation in endothelial cells
These findings highlight novel and essential roles of PFKFB4 (Montrer PFKFB4 Protéines) activity in later stages of neural crest (NC) development that are wired into the NC gene regulatory network.
Studied the effects of microRNA-27a on myogenin (Montrer MYOG Protéines) expression and the Akt/FoxO1 (Montrer FOXO1 Protéines) signal pathway during porcine myoblast differentiation. Overexpression of miR (Montrer MYLIP Protéines)-27a suppressed myogenin (Montrer MYOG Protéines) expression during porcine myoblast differentiation, whereas inhibition of miR (Montrer MYLIP Protéines)-27a promoted the mRNA and protein expression levels of myogenin (Montrer MYOG Protéines); overexpression of miR (Montrer MYLIP Protéines)-27a decreased the level of P-Akt/Akt and increased the protein level of FoxO1 (Montrer FOXO1 Protéines).
SCF (Montrer KITLG Protéines) is a critical regulatory factor for conceptus development and implantation during pregnancy in pigs.
These results indicate glycine enhances muscle protein mass under an inflammatory condition. The beneficial roles of glycine on the muscle are closely associated with maintaining Akt-mTOR-FOXO1 signaling and suppressing the activation of TLR4 and/or NOD2 signaling pathways.
Data show that homocysteine (Hcy) can ameliorate the endothelium-independent hypoxic coronary vasoconstriction, in which the inhibition of PI3K/Akt signaling pathway may be involved.
In pigs, lactose synthesis was significantly elevated with the increase of milk production and AKT1 could positively regulate lactose synthesis.
In conclusion, our observations reveal that PRRSV triggers the activation of FAK-PI3K-AKT-Rac1 signaling pathway to facilitate its entry into cells.
Host PI3K and Akt1 play a role in viral gene expression, leading to an increase in porcine reproductive and respiratory syndrome virus replication.
Activity of AKT is not essential for induction of germinal vesicle breakdown in porcine oocytes but plays a substantial role during progression of meiosis to MI/MII-stage.
IL-4 induced activation of Akt/SREBP-1/lipid biosynthesis in EC, resulting in protection against membrane attack complex and melittin, in association with mitochondrial protection.
findings show that megalin (Montrer LRP2 Protéines) is the sensor that determines whether cells will be protected or injured by albumin (Montrer ALB Protéines); it binds protein kinase B (PKB) in a D-3-phosphorylated phospholipid-insensitive manner, anchoring PKB in the luminal plasma membrane [
CIPK23 and AtKC1 exhibit distinct effects; however, they act synergistically and balance K(+) uptake/leakage to modulate AKT1-mediated low potassium responses in Arabidopsis.
results suggest that NO decreases K(+) absorption by promoting the synthesis of vitamin B6 PLP (Montrer FNTA Protéines), which further represses the activity of K(+) channel (Montrer KCNC4 Protéines) AKT1 in Arabidopsis.
Examination of the athak5 atakt1 double mutant, revealing novel aspects of an uptake system as yet unidentified by genetic means.
AKT1 is regulated by CIPK23 in guard cells and is involved in water stress responses.
These findings provide further insights into the signaling network consisting of CBL (Montrer CBL Protéines)-CIPK-PP2C interactions in the activation of the AKT1 channel.
Electrophysiological results showed that AtKC1 inhibited the AKT1-mediated inward K(+) currents and negatively shifted the voltage dependence of AKT1 channels.
AtHAK5 and AKT1 are vital for plant growth and development at low K+ concentrations.
In the range between 0.01 and 0.05 mM K+ AtHAK5 and AtAKT1 are the only contributors to K+ acquisition. At higher K+ concentrations, unknown systems come into operation and participate together with AtAKT1 in low-affinity K+ uptake.
CIPK23 directly phosphorylates the K+ transporter AKT1
Data show that interacting calcium sensors (CBL1 and CBL9) together with CIPK23, but not either alone, activated the AKT1 channel in a Ca(2 (Montrer CA2 Protéines)+)-dependent manner, connecting the Ca(2 (Montrer CA2 Protéines)+) signal to K(+) uptake through activation of a K(+) channel (Montrer KCNC4 Protéines).
the LIN-28/let-7/AKT/DAF-16 axis is a program that plays an important role in balancing reproduction and somatic maintenance.
this study shows that akt-1 and akt-2 negatively regulate DNA-damage-induced apoptosis in the C. elegans germline and the antiapoptotic activity of akt-1 is independent of its target gene daf-16 but dependent on cep-1/p53 (Montrer TP53 Protéines).
Modulation of pptr-1 affects insulin (Montrer INS Protéines)/IGF-1 (Montrer IGF1 Protéines) signaling pathway-associated phenotypes including life span, dauer, stress resistance, and fat storage; study shows that PPTR-1 functions by regulating worm AKT-1 phosphorylation at Thr (Montrer TRH Protéines) 350.
Exogenous AKT was transcribed, and AKT was overexpressed, inducing the phosphorylation of p70S6K (Montrer RPS6KB1 Protéines) (Thr389) and 4E-BP1 (Montrer EIF4EBP1 Protéines) (Thr37/46) in goat fetal fibroblasts.
findings suggested that the expressions of the cardiac CACNA1C (Montrer CACNA1C Protéines) were under the CLOCK-BMAL1 (Montrer ARNTL Protéines) regulation, probably through the PI3K-Akt signal pathway
This study has identified Akt as a novel intracellular pathway required for neural crest differentiation.
Overexpression of human Akt1 enhances adipogenesis and leads to lipoma formation in zebrafish.
The serine-threonine protein kinase encoded by the AKT1 gene is catalytically inactive in serum-starved primary and immortalized fibroblasts. AKT1 and the related AKT2 are activated by platelet-derived growth factor. The activation is rapid and specific, and it is abrogated by mutations in the pleckstrin homology domain of AKT1. It was shown that the activation occurs through phosphatidylinositol 3-kinase. In the developing nervous system AKT is a critical mediator of growth factor-induced neuronal survival. Survival factors can suppress apoptosis in a transcription-independent manner by activating the serine/threonine kinase AKT1, which then phosphorylates and inactivates components of the apoptotic machinery. Mutations in this gene have been associated with the Proteus syndrome. Multiple alternatively spliced transcript variants have been found for this gene.
, RAC-alpha serine/threonine-protein kinase
, protein kinase B alpha
, proto-oncogene c-Akt
, rac protein kinase alpha
, AKT1 kinase
, protein kinase B-alpha
, proto-oncogene c-AKT
, related to A and C kinases
, Akt kinase
, dAkt kinase
, protein kinase B
, related to PKA to PKC protein kinases
, related to the A and C kinases
, actin, cytoplasmic 1
, gamma non-muscle actin
, RAC protein kinase alpha RAC-PK alpha
, murine thymoma viral (v-akt) oncogene homolog 1
, thymoma viral proto-oncogene 1
, v-akt murine thymoma viral oncogene-like protein 1
, serine/threonine protein kinase
, protein kinase Akt-1
, protein kinase B, alpha
, v-akt murine thymoma viral oncogene homolog 1
, v-akt murine thymoma viral oncogene-like 1