IndraLab
Statements
sparser
"Its major effects are mediated by phosphorylation of proteins involved in the regulation of protein synthesis such as 4EBP1 and p70S6K, with subsequent phosphorylation of ribosomal S6 protein by p70S6K, and the components of ULK1 kinase that play a critical role in the regulation of autophagy [ xref ]."
sparser
"A recent bioinformatics study performed KEGG analysis and gene set enrichment analysis (GSEA) via Gene Expression Profiling Interactive Analysis (GEPIA) based on The Cancer Genome Atlas (TCGA) datasets and demonstrated that ACTL6A significantly affects ribosomal pathways. xref Since S6 kinase (S6K1) is a key member of the pathway, that participates in translational control, and the S6 kinase (S6K1)-S6 signaling pathway is critical for regulating proliferation and survival in response to growth factors, we focused on S6K1 as a downstream target of ACTL6A. xref S6K1 always phosphorylates S6 protein at Ser235, Ser236, Ser240, Ser244, and Ser247. xref Aberrant upregulation of S6 phosphorylation and increased S6K activity are frequently present in various tumors including ESCC. xref Although phosphorylated-ribosomal protein S6 (p-S6) is considered to be a potential target in ESCC in vitro and S6 phosphorylation has prognostic significance in ESCC, the relationship between S6 and ACTL6A remains unclear. xref "
"A knockin mouse carrying mutations at all phosphorylation sites in the primary s6k substrate, ribosomal protein s6 (rps6), has provided insight into the physiological role of this protein phosphorylation event. Of the many known substrates of s6k1, it is rps6 that has been shown to be directly involved, via its phosphorylation, in controlling cell size."
sparser
"A recent bioinformatics study performed KEGG analysis and gene set enrichment analysis (GSEA) via Gene Expression Profiling Interactive Analysis (GEPIA) based on The Cancer Genome Atlas (TCGA) datasets and demonstrated that ACTL6A significantly affects ribosomal pathways. xref Since S6 kinase (S6K1) is a key member of the pathway, that participates in translational control, and the S6 kinase (S6K1)-S6 signaling pathway is critical for regulating proliferation and survival in response to growth factors, we focused on S6K1 as a downstream target of ACTL6A. xref S6K1 always phosphorylates S6 protein at Ser235, Ser236, Ser240, Ser244, and Ser247. xref Aberrant upregulation of S6 phosphorylation and increased S6K activity are frequently present in various tumors including ESCC. xref Although phosphorylated-ribosomal protein S6 (p-S6) is considered to be a potential target in ESCC in vitro and S6 phosphorylation has prognostic significance in ESCC, the relationship between S6 and ACTL6A remains unclear. xref "
"A knockin mouse carrying mutations at all phosphorylation sites in the primary s6k substrate, ribosomal protein s6 (rps6), has provided insight into the physiological role of this protein phosphorylation event. Of the many known substrates of s6k1, it is rps6 that has been shown to be directly involved, via its phosphorylation, in controlling cell size."
sparser
"A recent bioinformatics study performed KEGG analysis and gene set enrichment analysis (GSEA) via Gene Expression Profiling Interactive Analysis (GEPIA) based on The Cancer Genome Atlas (TCGA) datasets and demonstrated that ACTL6A significantly affects ribosomal pathways. xref Since S6 kinase (S6K1) is a key member of the pathway, that participates in translational control, and the S6 kinase (S6K1)-S6 signaling pathway is critical for regulating proliferation and survival in response to growth factors, we focused on S6K1 as a downstream target of ACTL6A. xref S6K1 always phosphorylates S6 protein at Ser235, Ser236, Ser240, Ser244, and Ser247. xref Aberrant upregulation of S6 phosphorylation and increased S6K activity are frequently present in various tumors including ESCC. xref Although phosphorylated-ribosomal protein S6 (p-S6) is considered to be a potential target in ESCC in vitro and S6 phosphorylation has prognostic significance in ESCC, the relationship between S6 and ACTL6A remains unclear. xref "
reach
"P70 S6K phosphorylates the ribosomal protein S6 (rpS6), resulting in increased translation of mRNAs containing a 5 ' olygopyrimidine tract, whereas phosphorylation of 4E-BP1 by mTOR relieves inhibition on the initiation factor eIF4E resulting in more efficient cap dependent translation XREF_BIBR."
reach
"P70 S6K phosphorylates the ribosomal protein S6 (RPS6), resulting in increased translation of mRNAs containing a 5 ' oligopyrimidine tract, whereas phosphorylation of 4E-BP1 by mTOR relieves inhibition on the initiation factor eIF4E, resulting in more efficient cap dependent translation."
reach
"Upon activation by receptor tyrosine kinases or G protein coupled receptors, AKT activates mTOR, which in turn stimulates protein translation through inhibitory phosphorylation of eukaryotic translational initiation factor eIF4E binding protein 1 (4E-BP1) that inhibits eIF4E, and activating phosphorylation of p70S6 kinase (S6K) that phosphorylates ribosomal S6 protein."
rlimsp
"Ribosomal protein (rp) S6 is a component of the 40S ribosomal subunit that becomes phosphorylated at several serine residues upon mitogen stimulation, but the exact molecular mechanisms regulating its phosphorylation and the function of phosphorylated rpS6 is poorly understood. Here, we provide evidence that activation of the p90 ribosomal S6 kinases (RSKs) by serum, growth factors, tumor promoting phorbol esters, and oncogenic Ras is required for rpS6 phosphorylation downstream of the Ras/ERK signaling cascade. We demonstrate that while ribosomal S6 kinase 1 (S6K1) phosphorylates rpS6 at all sites, RSK exclusively phosphorylates rpS6 at Ser(235/236) in vitro and in vivo using an mTOR-independent mechanism."
reach
"mTORC1 controls mRNA translation via at least two well-established downstream targets: p70S6 kinase (p70S6K), which phosphorylates several translation factors including the ribosomal protein S6 (pS6), and repressor proteins of eukaryotic initiation factor 4E (eIF4E) termed 4E-BPs [5]."
reach
"mTORC1 controls mRNA translation via at least two well-established downstream targets: p70S6 kinase (p70S6K), which phosphorylates several translation factors including the ribosomal protein S6 (pS6), and repressor proteins of eukaryotic initiation factor 4E (eIF4E) termed 4E-BPs [5]."
sparser
"A recent bioinformatics study performed KEGG analysis and gene set enrichment analysis (GSEA) via Gene Expression Profiling Interactive Analysis (GEPIA) based on The Cancer Genome Atlas (TCGA) datasets and demonstrated that ACTL6A significantly affects ribosomal pathways. xref Since S6 kinase (S6K1) is a key member of the pathway, that participates in translational control, and the S6 kinase (S6K1)-S6 signaling pathway is critical for regulating proliferation and survival in response to growth factors, we focused on S6K1 as a downstream target of ACTL6A. xref S6K1 always phosphorylates S6 protein at Ser235, Ser236, Ser240, Ser244, and Ser247. xref Aberrant upregulation of S6 phosphorylation and increased S6K activity are frequently present in various tumors including ESCC. xref Although phosphorylated-ribosomal protein S6 (p-S6) is considered to be a potential target in ESCC in vitro and S6 phosphorylation has prognostic significance in ESCC, the relationship between S6 and ACTL6A remains unclear. xref "
sparser
"A recent bioinformatics study performed KEGG analysis and gene set enrichment analysis (GSEA) via Gene Expression Profiling Interactive Analysis (GEPIA) based on The Cancer Genome Atlas (TCGA) datasets and demonstrated that ACTL6A significantly affects ribosomal pathways. xref Since S6 kinase (S6K1) is a key member of the pathway, that participates in translational control, and the S6 kinase (S6K1)-S6 signaling pathway is critical for regulating proliferation and survival in response to growth factors, we focused on S6K1 as a downstream target of ACTL6A. xref S6K1 always phosphorylates S6 protein at Ser235, Ser236, Ser240, Ser244, and Ser247. xref Aberrant upregulation of S6 phosphorylation and increased S6K activity are frequently present in various tumors including ESCC. xref Although phosphorylated-ribosomal protein S6 (p-S6) is considered to be a potential target in ESCC in vitro and S6 phosphorylation has prognostic significance in ESCC, the relationship between S6 and ACTL6A remains unclear. xref "