IndraLab

Statements


MTOR phosphorylates RPS6KB1 on serine. 6 / 6
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rlimsp
"Serine/threonine kinase, mTOR, might phosphorylate and activate its downstream p70S6K and eIF4E-binding protein 1 (4E-BP1), both of which are key regulators of mRNA translation, including HIF-1α and cyclin D1 (Deng )."

reach
"In a previous study, we showed that mTOR could phosphorylate p70S6K at Thr 421/Ser 424, a specific site of ERK and inversely, ERK could phosphorylate p70S6K at Thr 389 controlled by mTOR signalling (L[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

rlimsp
"This is in line with our previous observation of a mechanism that appears to be two-pronged, whereby raptor, binding to the TOS motif of ERα, facilitates direct phosphorylation by mTOR on S104/106 and mTOR-activated kinase S6K1 phosphorylates ERα on S167 of the activation function 1 domain [15, 18, 33], promoting ERα activation."

rlimsp
"S104/106 are proline-directed sites, while S118 resides within a sequence that resembles a hydrophobic motif, which are phosphorylated by mTOR in its substrates 4E-BP1 and S6K1, respectively (Reviewed in 34, 35)."

rlimsp
"S6K1 is a serine/threonine kinase phosphorylated and activated by mTOR, and is overexpressed and highly activated in the spinal cord of ALS patients and in transgenic mice with the SOD1G93A gene."

rlimsp
"The S6K activation begins with the phosphorylation of serine residues in the C-terminal domain that expose the internal region of the protein, allowing mTOR to phosphorylate Thr389 in S6K1 and Thr388 in S6K2."