IndraLab

Statements


MTOR phosphorylates EIF4EBP1 on threonine. 9 / 9
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sparser
"It was shown that mTOR phosphorylated 4E-BP1 at serine and threonine residues in insulin-stimulated human embryonic kidney cells and these phosphorylations are inhibited by rapamycin [ xref ]."

reach
"Interestingly, there is evidence that mTOR directly phosphorylates 4E-BP1 at threonine 37/46."

sparser
"The interaction of 4E-BP1 with eIF4E is negatively regulated by mammalian target of rapamycin (mTORC1)-dependent phosphorylation of serine and threonine residues on 4E-BP1."

reach
"4EBP1 is phosphorylated by mTOR at serine 65 and threonine 70."

reach
"MTOR phosphorylated PHAS-I on serine and threonine residues in vitro, and these modifications inhibited the binding of PHAS-I to eIF-4E."

reach
"4EBP1 is phosphorylated by mTOR at serine 65 and threonine 70 XREF_BIBR."

reach
"It was shown that mTOR phosphorylated 4E-BP1 at serine and threonine residues in insulin stimulated human embryonic kidney cells and these phosphorylations are inhibited by rapamycin [XREF_BIBR]."

sparser
"MTOR phosphorylated PHAS-I on serine and threonine residues in vitro, and these modifications inhibited the binding of PHAS-I to eIF-4E. These studies define a role for mTOR in translational control and offer further insights into the mechanism whereby rapamycin inhibits G1-phase progression in mammalian cells."

reach
"When 4E-BP1 is phosphorylated by mTOR, first at critical priming threonine (T) 37 and T46 residues and then at other sites, 4E-BP1 is inactivated and releases eIF4E to allow initiation of cap dependent translation."