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EIF3F binds MTOR. 21 / 21
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"Importantly, the authors also found that the interaction between mTOR and eIF3f increased at the cell membrane after exercise and this response was enhanced in a fed state (20g protein / 40 g carbohydrate / 1 g fat) [XREF_BIBR]."
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"Under normal conditions, inactive S6K1 is bound to eIF3f and, upon mitogenic stimulation, MTOR binds to eIF3f and then phosphorylates and activates S6K1 (Csibi et al. 2008)."
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"The proximity of S6K1 and 4E-BP1 binding sites on MTOR could allow the interaction of the latter with eIF3f and MTOR complex (Marabita et al. 2016)."
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"Inactive S6K1 is bound to eIF3f, and upon amino acid/growth factor/mitogen stimulation, mTOR binds to eIF3f, leading to the phosphorylation and activation of S6K1 ( xref , xref )."
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"This reduction in mammalian target of rapamycin (mTOR) kinase activity was associated with reduced eIF3f and binding of both Raptor and eIF4G to eIF3."
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"Indeed association of eIF3f with mTOR and its activation is correlated with S6K1 activation and its respective dissociation from eIF3f."
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"Interestingly, the magnitude of association between mTOR and eIF3F was ~ 20% greater in the FED group 1h post exercise compared to CON, suggesting that this process is sensitive to post-exercise nutrition."
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"Interestingly, the interaction between mTOR and eIF3F was greater if resistance exercise was followed by a protein-carbohydrate beverage, compared with the exercise bout in isolation."
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"MTOR interacts with the C-terminal domain of eIF3f, a region recently shown to be critical for proper eIF3f activity in skeletal muscle xref ."
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"During the muscle cell growth, eIF3f interacts with mTOR and S6K1 to promote the assembly of the translation initiation complex and is degraded by MAFbx."
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"Interestingly, a protein–carbohydrate beverage post-exercise does not alter MTORC1/eIF3f translocation but increases the interaction between MTOR and eIF3f [ xref ], an association well recognized to drive MTORC1 activation and enhance MTOR target activity [ xref ]."
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"To map the domain of eIF3f that interacts with mTOR, the same panel of deletion mutants of eIF3f was cotransfected with an expression vector encoding HA-tagged mTOR in mouse primary muscle cells."
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"Indeed, mTOR/raptor complex bound to the scaffold protein eIF3f during muscle hypertrophy, which phosphorylated S6K1 and regulated downstream effectors of mTOR (51)."
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"Inactive S6K1 is bound to eIF3f, and upon amino acid and growth factor and mitogen stimulation, mTOR binds to eIF3f, leading to the phosphorylation and activation of S6K1."
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"Importantly, the authors also found that the interaction between mTOR and eIF3f increased at the cell membrane after exercise and this response was enhanced in a fed state (20g protein/ 40 g carbohydrate/ 1 g fat) [ xref ]."
| PMC
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"Using a muscle specific raptor KO mouse, Bentzinger et al. (2008) found a 4-19% reduction in muscle mass similar to the muscle mass reduction observed in eIF3F +/- mice, supporting a moderate but effective contribution of MTOR and eIF3f interaction in basal skeletal muscle mass of heterozygous mice.With muscle mass homeostasis resulting from a delicate balance between protein synthesis and degradation, a difference between protein synthesis rate and muscle mass can also result from altered protein breakdown pathways."
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