IndraLab

"After stimulation, S6K1 phosphorylates S6 on five serine residues (S235, S236, S240, S244, and S247) within the C-terminus [ xref ]."

"After stimulation, S6K1 phosphorylates S6 on five serine residues (S235, S236, S240, S244, and S247) within the C-terminus [XREF_BIBR]."

"P70S6K subsequently phosphorylates the S6 ribosomal protein on Ser (235)/Ser (236) and Ser (240)/Ser (244) to promote initiation of mRNA translation."

"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."

"In T cells, rpS6 is phosphorylated on 5 evolutionarily conserved serine residues by S6K1, and to a lesser extent by other AGC kinases including the p90 ribosomal S6 kinases (RSKs) ( xref ), in response to TCR/costimulation and cytokine and nutrient signaling pathways."

"Activated p70S6 kinase phosphorylates the 40S ribosomal S6 protein on serine residues, enabling mRNA translation."

"In T cells, rpS6 is phosphorylated on five evolutionarily conserved serine residues by S6K1 and to a lesser extent by other AGC kinases including the p90 ribosomal S6 kinases ( xref ) in response to TCR/costimulation and cytokine and nutrient signaling pathways."