IndraLab
Statements
"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
"P70 S6K1 is activated by two phosphorylation events: phosphorylation on Ser473 by mTOR complex 2 and on Thr308 by PDK1. xref , xref Subsequently, phosphorylated p70 S6K1 activates the ribosomal protein S6 that stimulates the translation of 5′-TOP messenger ribonucleic acids (mRNAs)."
reach
"Considering that (i) p70S6K induces S6 phosphorylation of the 40S ribosomal subunit, an essential condition for protein synthesis; (ii) eIF2 is essential for the initiation of messenger RNA translation process; and (iii) eIF5A and eEF1A play a central role in the elongation of the polypeptidic chain during the transcripts decoding, the data presented here lead us to suppose that a part of T3 induced insulin expression in INS-1E cells depends on the protein synthesis activation at the post-transcriptional level, as these proteins of the translational machinery were shown to be regulated by T3."
"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."
reach
"We observed a potential activation of translation in both the ischemic and non ischemic myocardial territories of the HC group, including lower levels of HIF-1alpha, in conjunction with higher S6K1 levels, which activates the ribosomal protein S6, in the ischemic myocardial territory (XREF_SUPPLEMENTARY)."
reach
"Overexpression of wild-type (WT) p70S6K1, and particularly F5A-E389-R3A and E389-DeltaCT, abrogated the reduction of p-S6 by rapamycin; however, rapamycin was equally potent in increasing the level of p-Akt in these cells transfected with empty vector, WT p70S6K1, or mutant p70S6K1, regardless of whether p70S6K signaling was inhibited or not (XREF_FIG)."
sparser
"S6K1 and S6K2 phosphorylate and activate the 40S ribosomal protein
S6, which promotes protein synthesis through an increased rate of
mRNA transcription. xref S6K1 also regulates
cell size and progression through the cell cycle, xref − xref in addition
to promoting cell survival by inactivating the proapoptotic protein
BAD. xref "
reach
"Changes in S6 phosphorylation are associated with activation of the mammalian target of rapamycin (mTOR) signaling cascade; mTOR activates the translational regulator ribosomal protein S6 kinase 1 (S6K1), which in turn activates ribosomal protein S6 by phosphorylation at serine S240/244."