IndraLab

Statements


MTOR phosphorylates EIF4EBP1 on T36. 15 / 16
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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."

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."

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."

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."

"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"

"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."

reach
"Current evidence suggests that mTOR phosphorylates 4E-BP1 on two residues, Thr36 and Thr45 [33] ."

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."

sparser
"Recent findings suggests that Thr36 and Thr45 in PHAS-I are preferentially phosphorylated by mTOR [14] ."

rlimsp
"mTAb1-activated mTOR phosphorylated Thr36, Thr45, Ser64, Thr69, and Ser82 in PHAS-I."

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
"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]"

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."

"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."

sparser
"Current evidence suggests that mTOR phosphorylates 4E-BP1 on two residues, Thr36 and Thr45 [33] ."