Sentence examples for major mTOR substrate from inspiring English sources

Consistent with this hypothesis, hypoxia, much like rapamycin, suppressed phosphorylation of the S6 ribosomal protein, a major mTOR substrate.

Next we investigated the activation of the major mTOR substrate, the Ser/Thr kinase p70 S6K1 which itself is important for the phosphorylation of the ribosomal protein S6 involved in mRNA translation.

Even in the absence of exogenous growth factors, mTOR activity remained remarkably elevated in glucose-fed cells 24 hours after serum withdrawal, as revealed by the phosphorylation patterns of the major mTOR effectors S6 kinase and 4E-BP1, and of the downstream substrate S6.

Activation of mTOR can be monitored by phosphorylation of its downstream targets and so we looked at the mTOR substrate p70-S6Kinase (p70S6K) and its substrate ribosomal protein S6 (rpS6) due to their established role directly downstream of the mTOR kinase.

To confirm that mTOR was inhibited in RAD001-treated mice, we examined the phosphorylation status of the downstream mTOR substrate ribosomal-S6 protein by immunohistochemistry with a widely-used phosphospecific antibody to Ser235/236 (pSer235/236

Mice with deletion of the mTOR substrate ribosomal S6 protein kinase (S6K) have increased lifespan [ 67].

Rapamycin only treated glands showed no expression of mTOR substrate activity, identical to unoperated controls.

These results clearly demonstrate that TFEB is an mTOR substrate and that S142 is a key residue for the phosphorylation of TFEB by mTOR.

Indeed, starvation of both control fibroblasts and wild-type mice leads to decreased phosphorylation (at the mTOR site) of the mTOR substrate p70S6 kinase (a conventional readout for mTOR kinase activity) (Fig.  4).

Immunoblot analysis confirmed mTOR inhibition by KU and EBSS, as indicated by a loss of ULK1 phosphorylation at the mTOR site (serine 757) and increased electrophoretic mobility (due to loss of phosphorylation) of another known mTOR substrate, 4E-BP1.

Satisfyingly, the phospho-S550 kinetics closely matched the UVRAG band shift as well as that of the known mTOR substrates 4E-BP1 and p70S6K, showing that UVRAG behaves as a conventional mTOR substrate.