IndraLab

Statements

MTOR phosphorylates EIF4EBP1 on T36. 13 / 14
3 | 2 4 4
sparser
"The present study has confirmed that mTOR (or a tightly associated kinase) phosphorylates 4E-BP1 at T 36 and/or T 45 and has identified an mTOR-associated kinase which phosphorylates 4E-BP1 within a[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
10471835
sparser
"RAFT1 phosphorylation of 4E-BP1 on Thr-36 and Thr-45 blocks its association with the cap-binding protein, eIF-4E, in vitro, and phosphorylation of Thr-45 seems to be the major regulator of the 4E-BP1-eIF-4E interaction in vivo."
9465032
reach
"MTOR readily phosphorylated T36 PHAS-I and T45 PHAS-I under conditions in which S64 PHAS-I, T69 PHAS-I, and S82 PHAS-I were not significantly phosphorylated."
10405182
sparser
"Recent findings suggests that Thr36 and Thr45 in PHAS-I are preferentially phosphorylated by mTOR [14] ."
10405182
rlimsp
"mTAb1-activated mTOR phosphorylated Thr36, Thr45, Ser64, Thr69, and Ser82 in PHAS-I."
9405468
signor
"Mtorc1 promotes protein synthesis by phosphorylating the eukaryotic initiation factor 4e (eif4e)- binding protein 1 (4e-bp1) and the p70 ribosomal s6 kinase 1 (s6k1). Raft1 phosphorylation of 4e-bp1 on thr-36 and thr-45 blocks its association with the cap-binding protein, eif-4e,in vitro. in response to insulin and nutrients, mtorc1, consisting of mtor, raptor (regulatory-associated protein of mtor), and mlst8, is activated and phosphorylates eukaryotic initiation factor 4e-binding protein (4ebp) and p70 s6 kinase to promote protein synthesis and cell size."
9465032
rlimsp
"RAFT1 phosphorylation of 4E-BP1 on Thr-36 and Thr-45 blocks its association with the cap-binding protein, eIF-4E, in vitro, and phosphorylation of Thr-45 seems to be the major regulator of the 4E-BP1-eIF-4E interaction in vivo."
9465032
reach
"RAFT1 phosphorylation of 4E-BP1 on Thr 36 and Thr 45 blocks its association with the cap binding protein, eIF-4E, in vitro, and phosphorylation of Thr 45 seems to be the major regulator of the 4E-BP1-eIF-4E interaction in vivo."
9465032
signor
"Specifically as part of mTORC1, mTOR directly phosphorylates the ribo- somal 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"
20670887
rlimsp
"Both (S/T)P sites, such as Thr36, Thr45, and Thr69 in PHAS-I and the h(S/T)h site (where h is a hydrophobic amino acid) Thr389 in p70(S6K), were phosphorylated. Rapamycin-FKBP12 inhibited mTOR activity. Surprisingly, the extent of inhibition depended on the substrate. Moreover, mutating Ser2035 in the rapamycin-binding domain (FRB) not only decreased rapamycin sensitivity as expected but also dramatically affected the sites phosphorylated by mTOR."
12370290
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."
9405468
signor
"In response to insulin and nutrients, mTORC1, consisting of mTOR, raptor (regulatory-associated protein of mTOR), and mLST8, is activated and phosphorylates eukaryotic initiation factor 4E-binding protein (4EBP) and p70 S6 kinase to promote protein synthesis and cell size."
17510057
rlimsp
"We also measured the phosphorylation of the T36/45 residues on 4E-BP1. Importantly, numerous studies have shown that mTOR can directly phosphorylate these residues [42], [43], but much to our surprise, neither mechanical stimulation, nor U0126, altered the amount of T36/45 phosphorylation."
23077579