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Validated All-in-One™ qPCR Primer for RPS6KB1(NM_003161.3) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
This gene encodes a member of the RSK (ribosomal S6 kinase) family of serine/threonine kinases. This kinase contains 2 non-identical kinase catalytic domains and phosphorylates several residues of the S6 ribosomal protein. The kinase activity of this protein leads to an increase in protein synthesis and cell proliferation. Amplification of the region of DNA encoding this gene and overexpression of this kinase are seen in some breast cancer cell lines. Alternate translational start sites have been described and alternate transcriptional splice variants have been observed but have not been thoroughly characterized. [provided by RefSeq].
Gene References into function
- TF cytoplasmic domain-independent stimulation of protein synthesis via activation of S6 kinase contributes to FVIIa effects in pathophysiology.
- Cdc2 provides a signal that triggers inactivation of S6K1 in mitosis.
- both p70S6K and Akt are activated in the majority of human papillary cancer cells
- Muscarinic receptors mediate activation of this enzymme in astrocytoma cells, coupled with pi 3-kinase activation.
- TNF-receptor activation leads to activation of the p70S6K; TRAF4 is a mediator in this TNF-induced signaling pathway; and TRAF4 inhibits Fas-induced apoptosis
- transient expression of the wild type Rheb1 or Rheb2 causes activation of p70S6K, while expression of Rheb1D60K mutant results in inhibition of basal level activity of p70S6K
- PI3K mediates G(1) progression and cyclin expression through activation of an AKT/mTOR/p70S6K1 signaling pathway in the ovarian cancer cells.
- the increase in basal phosphorylation of p70S6K upon granulocytic differentiation of myeloid leukemic cells and their responses to GM-CSF that are closely paralleled with tyrosyl phosphorylation of its receptor
- Akt and P70S6K phosphorylation and Gadd45 levels are modulated by GPx-1 in tumor cells
- autocrine TGFalpha regulates cell adhesion function by multiple signaling pathways via specific phosphorylation sites of S6K in cancer cells
- the response of muscle protein synthesis to insulin and amino acid is impaired in elderly humans; a defect in S6K1 pathway activation may be responsible for this alteration
- VEGF and HIF-1alpha expression are inhibited by SU5416 through the inhibition of PI3K/AKT/p70S6K1 pathway in ovarian cancer cells
- REVIEW: negative feedback of the PI3K-Akt pathway; one feedback loop composed of mTOR and ribosomal S6 kinase blocks further activation of the pathway through inhibition of insulin receptor substrate function
- Overexpression of ribosomal protein S6 kinase, 70kDa is associated with liver neoplasms
- RSPRR motif interacts with a negative regulator of S6K1 that is normally suppressed by mTOR.
- Ability of hyperinsulinaemia to increase mTOR/p70 S6K pathway activity and IRS-1/2 serine phosphorylation in a tissue-specific fashion.
- identified p70 S6 kinase as a major signal transduction pathway activated by OPN-1 during the migratory response in JAR cells
- S6 kinase 1 is essential for the control of muscle cytoplasmic volume by Akt and mTOR
- interferon alpha has a role in regulating the p70 S6 kinase pathway in chronic myelogenous leukemia cells
- Although zinc could induce cell proliferation and cell growth, and increased phosphorylation of neurofilaments, only cell growth appeared to be related to p7056kinase activation.
- p70S6 kinase is a major effector of mTOR phosphorylation at Ser-2448 in response to both mitogen- and nutrient-derived stimuli
- The mainly anti-apoptotic p70S6k signalling is downregulated in cellular and transgenic models of Alzheimer's disease and in peripheral cells of patients, and could contribute to the pathogenesis of the disease.
- hVps34 is a nutrient-regulated lipid kinase that integrates amino acid and glucose inputs to mTOR and S6K1
- These data suggest that PI3K-dependent T389/T229 phosphorylation is limiting in late-phase p70S6K activation by EGF and contributes to the cooperative effect of GPCRs on p70S6K activity and cell growth.
- S6K1 maneuvers on and off the eukaryotic initiation factor 3 translation initiation complex.
- mTOR nuclear import is required for its cytoplasmic signaling to S6K1
- We conclude that resistance exercise effectively increases the phosphorylation of S6K1 on Thr421/Ser424, which is not associated with a substantial increase in S6 phosphorylation in a fasted state.
- p70S6K activation induces expression of MMP-9 associated with hepatocyte growth factor-mediated invasion in human ovarian cancer cells
- both S6K1 and eukaryotic translation initiation factor 4E binding protein 1 pathways, regulated by TORC1, are required for cell motility
- The higher expressions of p-p70S6K was associated with worse outcome in glioblastoma.
- In the presence of urokinase plasminogen activator, overexpression of ganglioside GM3 paradoxically increases proliferation of carcinoma cells by augmenting ERK-independent p70S6 kinase activation.
- Inhibition of p70S6K1 activity by its siRNA also decreased cell migration, invasion, and proliferation associated with the induction of p27(KIP1) levels, and with the inhibition of cell cycle-associated proteins.
- These results suggest that p70S6K1 regulates turnover of HDM2 protein for cancer development.
- These studies suggest that, through serine phosphorylation, Raptor-mTOR and S6K1 promote the depletion of IRS1 from specific intracellular pools in pathological states of insulin and IGF-I resistance and in lesions associated with tuberous sclerosis.
- Collectively, these data suggested that acetaldehyde did not adversely affect glucose uptake despite inhibition of insulin signaling cascade at the levels of Akt and mTOR, possibly due to enhanced p70(S6K) phosphorylation.
- This study demonstrates a novel mechanism of EGF-induced VEGF and HIF-1alpha expression through production of H2O2 and activation of AKT and p70S6K1 in human ovarian cancer cells.
- S6K1 regulates GSK3 under conditions of mTOR-dependent feedback inhibition of Akt
- in response to mitogens, PDCD4 was rapidly phosphorylated by protein kinase S6K1 & then degraded by ubiquitin ligase SCF(betaTRCP); it is proposed that regulated degradation of PDCD4 in response to mitogens allows efficient protein synthesis & cell growt
- p70 S6 kinase activates PAK1 and contributes to phosphatidylinositol 3-kinase- and ERK-mediated regulation of HCV RNA replication
- Monitoring P70(S6K) phosphorylation can help predict and monitor the biological effectiveness of rapamycin in renal transplant recipients with Kaposi sarcoma.
- ERK cascade regulates motility of hepatocellular carcinoma cells via uPAR production and p70S6K phosphorylation.
- phosphorylation increased following low-intensity resistance exercise training combined with blood flow restriction
- The inhibition of Akt and S6K1 phosphorylation by PRR5 knock down correlates with reduction in the expression level of platelet-derived growth factor receptor beta (PDGFRbeta).
- PRAS40 acts downstream of mTORC1 but upstream of its effectors, such as S6K1 and 4E-BP1
- AKT amplification and the mTOR/p70S6K1 pathway play an important role in human lung cancer cells acquiring CDDP resistance
- HPV16 modifies S6 kinase activation via mechanism, which activates S6 kinase downstream of Akt function.
- Rapamycin inhibits S6K1-dependent IRS-1 serine phosphorylation, increases IRS-1 protein levels, and promotes association of tyrosine-phosphorylated IRS-1 with PI3K.
- Data show that URI and PP1gamma are components of an S6K1-regulated mitochondrial pathway dedicated to oppose sustained S6K1 survival signaling and to ensure that the threshold for apoptosis is set based on nutrient and growth factor availability.
- Cyclin G2 expression is modulated by HER2 signaling through multiple pathways including phosphoinositide 3-kinase, c-jun NH(2)-terminal kinase, and mTOR signaling.
- SKAR-mediated recruitment of activated S6K1 to newly processed mRNPs serves as a conduit between mTOR checkpoint signaling and the pioneer round of translation when cells exist in conditions supportive of protein synthesis.
- p70 S6K Thr 389 (ribosomal protein S6 kinase 70kDa polypeptide 1) phosphorylation was attenuated during resistance exercise
- Resistance exercise decreases eIF2Bepsilon phosphorylation and potentiates the feeding-induced stimulation of p70S6K1 and rpS6 in young men.
- Gene silencing of p70S6K by siRNA alters gene expression in two breast cancer cell lines.
- activation of the Akt-mTOR-p70S6K pathway plays a significant role in HCC progression by promoting neoangiogenesis.
- The role and molecular mechanism of p70S6K1 in regulating angiogenesis and tumor growth, and angiogenesis.
- S6K1 directly phosphorylates IRS-1 on Ser-270 to promote insulin resistance in response to TNF-(alpha) signaling through IKK2.
- These data suggest that the S6K1/4E-BP1 pathway may play an important role in polyploidization of megakaryocytes.
- Activation, regulation, and function of S6K1 isoforms was determined in breast cancer.
