IndraLab
Statements
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"Over expression of eIF4E can lead to increased cell proliferation, transformation and tumorigenesis. xref 4E-BP1, known as PHAS-1, normally binds eIF4E, inhibiting cap-dependent translation and is phosphorylated in vivo on multiple residues; phosphorylation by mTOR on Thr37 and Thr46 of human 4E-BP1 may be very important for subsequent phosphorylation. xref EIF4E protein levels were unchanged with the progression of cell series ( xref )."
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"Gels were transferred to nitrocellulose membranes and incubated with antibodies, diluted 1:1000 unless otherwise stated, directed to phosphorylated Ser2448 of mTOR, LAMP1, 4E-BP1, phosphorylated Thr 37 and Thr 46 of 4E-BP1, GAPDH, p70S6K, LAMP2 diluted 1:100 and beta-actin diluted 1:2000."
"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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"The mTOR kinase complex 1 (mTORC1), a downstream target of both AKT and ERK signaling [XREF_BIBR, XREF_BIBR], is a master regulator of eIF4E initiated cap dependent translation by phosphorylating 4E-BP1 on Thr37 and Thr46 that act as priming sites for its subsequent phosphorylation on Ser65 and Thr70 [XREF_BIBR]."
"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-BPs 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."