Foxo1 and Foxo3 help Foxp3.
Mitochondria and FOXO3: breath or die.
This was accompanied by increased phosphorylation of FOXO3.
SNPing at FOXO3 to limit inflammation.
Tolerogenic pDCs: spotlight on Foxo3.
Deacetylation of FOXO3 by SIRT1 or SIRT2 leads to Skp2-mediated FOXO3 ubiquitination and degradation.
The FOXO3 decreased after treatment with FOXO3 small interfering RNAs (siRNAs).
FoxO3 controls dangerous proteolytic liaisons.
Methylation of FoxO3 by Set9 decreases FoxO3 protein stability, while moderately increasing FoxO3 transcriptional activity.
The SIRT3-mediated deacetylation of FOXO3 further reduces FOXO3 phosphorylation, ubiquitination and degradation, thereby stabilizing FOXO3 proteins.
In this study, wild-type FOXO3 and FOXO3 mutated on Akt sites [FOXO3 T32A/S253A/S315A or TM (triple mutant)] were fused to the TAT-PTD.
It is thought that bovine primordial follicle activation is regulated by the FOXO3-dependent mechanism and that knockdown of FOXO3 induces the release of primordial follicles from FOXO3 ...
Specificity of the requirement for Foxo3 in primordial follicle activation.
FoxO3 controls autophagy in skeletal muscle in vivo.
FoxO1, FoxO3, and FoxO4 act redundantly as mediators of these effects.
Foxo3 is required for the regulation of oxidative stress in erythropoiesis.
Knockdown of FOXO3 induces primordial oocyte activation in pigs.
In this regard, the involvement of FOXO3, a forkhead transcription factor, was studied.
Further, siRNA was designed to knock down porcine FOXO3.
FoxO3 regulates neural stem cell homeostasis.
Within oocytes, Foxo3 is regulated by nucleocytoplasmic shuttling.
Tumor suppressor FOXO3 participates in the regulation of intestinal inflammation.
Methylation of FoxO3 regulates neuronal cell death.
Methylation by Set9 modulates FoxO3 stability and transcriptional activity.
Foxo3 is required to maintain the ovarian reserve in mice.
By 16 hours, nuclear FoxO3 is both phosphorylated and acetylated.
Human cartilage expressed FOXO1 and FOXO3 but not FOXO4 proteins.
FOXO3 functions as a transcriptional factor when it is localized in nuclei.
The role of FOXO3 in DNA damage response in thyrocytes.
Bimodal regulation of FoxO3 by AKT and 14-3-3.
FOXO3 knockdown accelerates development of bovine primordial follicles.
Posttranslational modifications control FoxO3 activity during denervation.
In addition, the absence of Foxo3 exacerbated the effects of the loss of Foxo1.
The FoxO3 transactivation is augmented by RASSF1A and the MST1 signaling pathway.
G17 also induced FOXO3 phosphorylation assessed by Western blots with anti-phospho-FOXO3 antibodies, and BAPTA-AM inhibited this effect.
Phosphorylation by AMPK leads to the activation of FOXO3 transcriptional activity without affecting FOXO3 subcellular localization.
FoxO3 controls the transcription of autophagy-related genes, including LC3 and Bnip3, and Bnip3 appears to mediate the effect of FoxO3 on autophagy.
The granulosa cells expressing FOXO3 coincided with apoptotic cells, indicating a role of FOXO3 as a proapoptotic factor in granulosa cells of porcine ovaries.
GILZ does not hinder FOXO3 DNA-binding activity and does not physically interact with FOXO3.
P8 expression represses FoxO3 transcriptional activity, and p8 knockdown affects FoxO3 nuclear localization.
Overexpression of Skp2 caused poly-ubiquitination of FOXO3 and degradation, whereas knockdown of Skp2 increased the amount of FOXO3 protein.
In the livers of mice deficient in SIRT1, we detected increased expression of FOXO3, indicating SIRT1 regulates FOXO3 protein levels in vivo.
Correlative analysis of FOXO3 and RNA polymerase II ChIP-seq profiles demonstrates FOXO3 to act as a transcriptional activator.
Collectively, these findings define a novel modification of FOXO3 and show that lysine methylation negatively regulates FOXO3-mediated transcription and neuronal apoptosis.
Foxo3 deficiency also led to a decrease in SIRT6, revealing the existence of LD and FOXO3 feedback regulation in colonic cells.
To test whether FOXO3 is protective for alcoholic liver injury, we fed alcohol to FOXO3(-/-) mice.
The FOXO3 expression is significantly reduced in CRC specimens compared with normal tissue, and progressive FOXO3 downregulation is associated with advancing pathological stage.
Silencing FOXO3 and Foxo3 with siRNAs abrogated the ability of human and mouse TADCs, respectively, to tolerize and induce suppressive activity by T cells.
While FoxO3 is not necessary for p53-dependent cell cycle arrest, FoxO3 appears to modulate p53-dependent apoptosis.
FoxO3 phosphorylation by AKT generates binding sites for 14-3-3, which in-turn regulates FoxO3 transcriptional activity and localization.
Here we show that FoxO3 is progressively acetylated during denervation and concomitantly atrogin-1, the bona fide FoxO3 target, is downregulated.
We wanted to study FoxO3 function in the adult heart in vivo by expressing a constitutively active mutant of FoxO3 in transgenic mice.
Moreover, inhibition of proliferation by overexpressing FOXO3 was not reversed by the EGFR signaling, implicating FOXO3 as one of the regulators downstream of EGFR.
Phosphorylation of FoxO3 via the AKT, IKK, and ERK pathways leads to deregulation, cytoplasmic retention, degradation of FoxO3 and favors tumor progression.
The variation identified in ovine FOXO3 may have an impact on both the structure and function of ovine FOXO3 and, consequently, affect the longevity of sheep.
Lipid extracts from black seeds inhibit FOXO3 activity and thereby modulate the expression of FOXO3-dependent genes.
Cell fractionation and immunofluorescence microscopy showed translocation of FOXO3 to the nucleus in BCG-infected cells, concomitantly with an increase of FOXO3 transcriptional activity.
After treatment for 6 h, OGD could reduce FoxO3 phosphorylation and promote FoxO3 in cytoplasm.
Knockdown of DEPP prevented the primary and secondary ROS wave during FOXO3 activation and attenuated FOXO3- and H2O2-induced apoptosis.
The miR-122 inhibited Foxo3 translation as assessed using an miR mimic, an inhibitor, and a Foxo3 3'-UTR reporter.
E2F1 attenuates FOXO3-mediated expression of MnSOD and Catalase without affecting FOXO3 protein stability, subcellular localization, or phosphorylation by Akt.
We propose that E2F1 inhibits FOXO3-dependent transcription by directly binding FOXO3 in the nucleus and preventing activation of its target genes.
SIRT1 had a dual effect on FOXO3 function: SIRT1 increased FOXO3's ability to induce cell cycle arrest and resistance to oxidative stress but inhibited FOXO3's ability to induce cell death.
Oocyte-specific ablation of Pten resulted in PI3K-induced Akt activation, Foxo3 hyperphosphorylation, and Foxo3 nuclear export, thereby triggering primordial follicle activation, defining the ...
Thus, in this study, we sought to determine the effect of 1) human term labor on myometrial FOXO3 expression and 2) FOXO3 inhibition and FOXO3 overexpression on proinflammatory and prolabor ...
Adoptive transfer of T helper cells or silencing of FOXO3 by siRNAs repressed the expression of FOXO3 gene and inhibited the tolerogenicity of TADCs. Therefore, inhibition of FOXO3 signals might ...
After knockdown of FOXO3 or expression of a dominant-negative FOXO3 mutant we observed that etoposide- and doxorubicin-induced elevation of cellular ROS depends on FOXO3 activation and induction ...
This suggests that if p16INK4A is deleted during leukemia development, FOXO3 levels elevate and FOXO3 has to be inactivated by deregulation of the PI3K-PKB pathway to prevent FOXO3-induced cell death.
mTOR, p-Akt(ser473), p-Akt(tjr308), Akt, p-FoxO3, FoxO3 in cytoplasm and nucleus, and total FoxO3 protein expression were detected by Western blot assay.
FOXO3 and FOXO4 genes are fused to MLL gene in hematological malignancies.
The functional significance of the interaction between FoxO3 and GC receptor was established in T lymphocytes.
In either case, we show that FoxO4 (but not FoxO3) is required as proapoptotic mediator.
We show that IL-2 regulates phosphorylation of FoxO3 in a PI3K-dependent fashion.
These results suggest that FL-induced regulation of apoptosis is executed by FoxO3.
Downstream of Akt: FoxO3 and mTOR in the regulation of autophagy in skeletal muscle.
Interestingly, Akt phosphorylation of MstI strongly inhibits its kinase activity on FOXO3.
Akt/PKB activation blocks FoxO3 activation and autophagy, and this effect is not prevented by rapamycin.
However, these rare sequence variants were not associated with significant decreases in FOXO3 activity.
In particular, Bnip3 induces autophagosome formation and is responsible for the induction of autophagy by FoxO3.
Also, inactivation of the gene coding for FoxO3 enhances insulin-dependent Akt phosphorylation.
The transcription of FOXO genes is stimulated by FOXO3 and repressed by growth factors.
FOXO3 is considered one of the molecules responsible for the dormancy of primordial oocytes in adult ovaries.
This study provides support that FoxO3 is a good biomarker for BCR-ABL-mediated leukemogenesis.
HADC6, p62, and FoxO3 may play an important role in mobilizing this proteolytic consortium.
Different roles of Foxo1 and Foxo3 in the control of endothelial cell morphology.
Moreover, GILZ exclusive cytoplasmic localization is a prerequisite for FOXO3 inhibition and relocalization.