IndraLab

Statements

RPS6KB1 binds EIF3F. 22 / 22
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sparser
"Because the phosphorylation of the hydrophobic motif at T389 in S6K1 has been shown to regulate the interaction between S6K1 and the eIF3-PIC complex xref , this prompted us to examine the phosphorylation state of S6K1 that physically interacts with eIF3f by using a GST pull down assay with total cellular extracts from normal myotubes and/or atrophied myotubes."
20126553
biogrid
No evidence text available
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reach
"S6K1 interacts with eIF3f and, in vitro, phosphorylates eIF3."
24396066
sparser
"During terminal muscle differentiation, eIF3f interacts with hypophosphorylated S6K1 through its MPN domain and with the mTOR/Raptor complex (mTORC1) by interacting with a TOS site contained in its C-terminal region [ xref ]."
26497985
sparser
"S6K1 interacts with eIF3f and, in vitro, phosphorylates eIF3."
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biogrid
No evidence text available
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sparser
"Altogether our data confirm that eIF3f connects mTOR kinase to S6K1 and the non-phosphorylated forms of S6K1 physically interact with eIF3f."
20126553
reach
"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 (Csibi et al., 2010; ."
23769948
reach
"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."
23769948
sparser
"As shown in xref , increasing amounts of the mutant (eIF3f 1–221) disrupted the activation of S6K1 by mTOR as evidenced by the decrease in both the S6K1 and rpS6 phosphorylation and an increase in hypophosphorylated form of S6K1 bound to eIF3f."
20126553
reach
"As shown in XREF_FIG, increasing amounts of the mutant (eIF3f 1-221) disrupted the activation of S6K1 by mTOR as evidenced by the decrease in both the S6K1 and rpS6 phosphorylation and an increase in hypophosphorylated form of S6K1 bound to eIF3f."
20126553
reach
"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."
23354061
sparser
"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 (Csibi et al., 2010, Holz and Blenis, 2005)."
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reach
"This work also showed that p70S6K1 interacts with, and phosphorylates eIF3f, leading the authors to suggest that p70S6K1 phosphorylates eIF3 to stimulate the Paip1-eIF3 interaction and promotes translation initiation."
25486193
sparser
"The Mov34 domain of eIF3f is able to associate with the hypophosphorylated form of S6K1 adds to the evidence of a physical association of eIF3f and S6K1 prior to S6K1 activation."
20126553
biogrid
No evidence text available
16286006
sparser
"As previously shown in xref , the non-phosphorylated form of S6K1 interacts with eIF3f."
20126553
reach
"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 (Csibi et al., 2010, Holz and Blenis, 2005)."
23769948
sparser
"Whether MAFbx interacts with free eIF3f or with eIF3f molecules bound to S6K1 still remains unclear."
23354061
sparser
"As shown in xref , we observed that the hypophosphorylated forms of S6K1 preferentially bound to eIF3f."
20126553
sparser
"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 )."
23769948
trips
"S6K1 interacts with eIF3f and, in vitro, phosphorylates eIF3."
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