IndraLab

Statements

EIF3F activates RPS6KB1. 10 / 10
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"Degradation of eIF3f by MAFbx Suppresses S6K1 Activation by mTOR."
20126553
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"The degradation of eIF3f suppresses S6K1 activation by mTOR in a MAFbx / atrogin-1-induced atrophy model ( Csibi et al ., 2010 ) ."
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"The degradation of eIF3f suppresses S6K1 activation by mTOR in a MAFbx/atrogin-1-induced atrophy model (Csibi et al., 2010)."
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"Here we present evidence that in MAFbx induced atrophy the degradation of eIF3f suppresses S6K1 activation by mTOR, whereas an eIF3f mutant insensitive to MAFbx polyubiquitination maintained persistent phosphorylation of S6K1 and rpS6."
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"Moreover inhibition of eIF3f degradation (mutant eIF3f K 5-10 R) in MAFbx induced atrophy maintained S6K1 activation by mTOR (XREF_FIG) and electroporation of eIF3f K 5-10 R expression vector in mice not only protects against muscle atrophy but also induces hypertrophy XREF_BIBR."
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"The degradation of eIF3f suppresses S6K1 activation by mTOR in a MAFbx and atrogin-1-induced atrophy model."
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"Only eIF3f with an intact TOS motif coimmunoprecipitates with mTOR-raptor (XREF_FIG) and activates mTOR-raptor and S6K1 pathway (XREF_FIG)."
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"Genetic repression of eIF3f in differentiated skeletal muscle is sufficient to induce atrophy XREF_BIBR and degradation of eIF3f by MAFbx suppresses S6K1 activation by mTOR."
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"To further confirm that eIF3f mediates activation of S6K1 by mTOR, an eIF3f mutant deleted of the C-terminal domain was transfected in mouse primary muscle cells and the phosphorylation of downstream targets of mTOR was assessed."
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"In contrast, eIF3f knockdown was sufficient to induce the repression of S6K1 activity and the lack of myogenic differentiation (XREF_FIG)."
20126553