
IndraLab
Statements
sparser
"Since eIF3f serves as a connecting platform between mTOR-raptor and S6K1 in
muscle cells ( xref ) and
mutation of the C-terminal lysines in eIF3f increases phosphorylation of S6K1,
we assessed the binding affinities of both eIF3f wt and mutant eIF3f
K 5–10 R proteins with S6K1 and mTOR-raptor."
reach
"In contrast, HA tagged eIF3f mutant K 5-10 R overexpressed in mouse primary myotubes at 4 th day of differentiation was able to bind both endogenous mTOR and raptor by about 2-fold higher than HA tagged eIF3f wt leading to a higher phosphorylation and activity of S6K1 as evidenced by an increased phosphorylation of rpS6 on Ser235/236 residues (XREF_FIG)."