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MTOR phosphorylates EIF4EBP1 on S65. 30 / 31
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"The RR-mTOR mice also enabled us to demonstrate that mTOR is necessary for mechanical stimulation to induce an increase in 4E-BP1 S64 phosphorylation, and a decrease in total 4E-BP1."

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"Here, we show that a functional TOS motif is required for 4E-BP1 to bind to raptor (a recently identified mTOR-interacting protein), for 4E-BP1 to be efficiently phosphorylated in vitro by themTOR/raptor complex, and for 4E-BP1 to be phosphorylated in vivo at all identified mTOR-regulated sites. mTOR/raptor regulated phosphorylation is necessary for 4E-BP’s efficient release from the translational initiation factor eIF4E. We find that the TOS motif is absolutely required for efficient phosphorylation of 4E-BP1 at all the identified mTOR-regulated sites, namely, Thr37/46, Ser65, and Thr70 in vivo."

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sparser
"mTAb1-activated mTOR phosphorylated Thr36, Thr45, Ser64, Thr69, and Ser82 in PHAS-I. All five of these sites fit a (Ser/Thr)-Pro motif and are dephosphorylated in response to rapamycin in rat adipocytes."

sparser
"In response to stimuli such as growth factors, hormones, nutrients, or increased energy levels, mTOR phosphorylates 4E-BP1 primarily at residues Ser65 and Thr73."

reach
"In response to stimuli such as growth factors, hormones, nutrients, or increased energy levels, mTOR phosphorylates 4E-BP1 primarily at residues Ser65 and Thr73."

sparser
"Consistent with this finding, experiments with purified proteins have shown that rapamycin/FKBP12 only partially inhibits the in vitro phosphorylation of 4EBP1 at Ser 65 by mTOR but can fully inhibit the in vitro phosphorylation of S6K [ xref ]."

rlimsp
"For example, mTOR can directly phosphorylate the 36/45 residues of 4E-BP1, and phosphorylation on these residues allows 4E-BP1 to become further phosphorylated on residues such as S64 [43], [63]."

sparser
"MTOR-dependent phosphorylation of serine Ser 65 and N-terminal Thr 37 , Thr 46 , and Thr 70 in 4E-BP1 cleaves 4E-BP1 from the translational activator eIF-4E ( xref )."

sparser
"4EBP1 is phosphorylated by mTOR at serine 65 and threonine 70 ( xref )."

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"PHAS-I in adipocytes and HEK293 cells is phosphorylated in the following five sites, all of which conform to a (S/T)P motif (9, 10): Thr-36, Thr-45, Ser-64, Thr-69, and Ser-82. Thr-45 and Ser-64 flank the eIF4E-binding motif (7, 8), and phosphorylation of either site blocks eIF4E binding in vitro (10, 11). Insulin stimulates the phosphorylation of Thr-36, Thr-45, Ser-64, and Thr-69 in both fat cells and HEK293 cells, and incubating cells with rapamycin decreases the phosphorylation of these sites.Immunoprecipitated epitope-tagged mammalian target of rapamycin (mTOR) phosphorylated Thr-36/45. mTOR also phosphorylated Thr-69 and Ser-64 but only when purified immune complexes were incubated with the activating antibody, mTAb1."

reach
"Growth factor mitogen or hormone stimulated mTOR activation mediates the downstream inhibitory phosphorylation of 4E-BP1 at Ser65 suppressing its ability to bind and inactivate the translation initiation factor eIF4E."

sparser
"We propose that meiotic phosphorylation of 4E-BP1 on Ser65 and Thr70 by mTOR acts to stimulate cap-dependent translation as the oocyte proceeds though meiosis (particularly after NEBD) and that specific localization of the key cap-dependent translation regulatory factors, xref is essential for the translation of specific mRNAs at the spindle area to ensure errorless meiotic progression."

reach
"In support of this model, the TOS motif 4E-BP1 mutant (4E-BP1-F114A) fails to coimmunoprecipitate with raptor, resulting in reduced in vitro phosphorylation of 4E-BP1 by mTOR and reduced phosphorylati[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Hyperphosphorylation of 4EBP1 by mTOR on Ser65 and Thr70 disrupts the binding of 4EBP1 to eIF4E and results in activation of cap dependent translation [XREF_BIBR, XREF_BIBR]."

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reach
"MTOR kinase activity phosphorylates (among other sites) Ser65 of 4E-BP1, Thr389 of S6K, and Ser473 of AKT [XREF_BIBR, XREF_BIBR]."

"These results indicate that arg, leu, and gln act coordinately to stimulate proliferation of ptr cells through activation of the mtor-rps6k-rps6-eif4ebp1 signal transduction pathway. Specifically as part of mtorc1, mtor directly phosphorylates the ribosomal protein s6 kinases (s6k1 and s6k2) and the eukaryotic initiation factor 4e (eif4e)-binding proteins (4e-bp1 and 4e-bp2), both of which control specific steps in the initiation of cap-dependent translation"

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sparser
"The work clarifies that phosphorylation of 4E-BP1 at Ser65 by mTOR is not required to inhibit 4E-BP1 binding to eIF4E and that rapamycin-insensitive mTOR-mediated phosphorylation at 4E-BP1 Thr46 is sufficient to inhibit 4E-BP1 binding to eIF4E. Phosphorylation at 4E-BP1 Thr37 is also shown to be rapamycin-insensitive."

sparser
"Hyperphosphorylation of 4EBP1 by mTOR on Ser65 and Thr70 disrupts the binding of 4EBP1 to eIF4E and results in activation of cap-dependent translation [ xref , xref ]."

reach
"Our data demonstrate that mTOR FAT domain mutants promote 4E-BP1 phosphorylation at the nutrient sensitive site Ser65 in the presence of nutrients."

sparser
"Our data demonstrate that mTOR FAT domain mutants promote 4E-BP1 phosphorylation at the nutrient sensitive site Ser65 in the presence of nutrients (Figure xref , xref )."