2005年12月9日 · After confirming the interaction between endogenous S6K1 and eIF3, the authors set upon uncovering potential mechanisms that regulate this interaction. They found that multiple stimuli, including growth factors and nutrients, disrupt the association of S6K1, but not the related S6K2, with eIF3 in a rapamycin-sensitive fashion.

2015年9月9日 · Here, we challenged cell size control through S6K1 by specifically depleting its binding partner eIF3 in normal and transformed cell lines. We show that loss of eIF3 leads to a massive reduction of cell size and cell number accompanied …

2022年3月12日 · Here, we show that eIF3a regulates S6K1 activity by inhibiting mTORC1 kinase via regulating Raptor synthesis. The regulation of Raptor synthesis is via eIF3a interaction with HuR (human antigen...

2005年11月18日 · We show that mTOR and S6K1 maneuver on and off the eukaryotic initiation factor 3 (eIF3) translation initiation complex in a signal-dependent, choreographed fashion. When inactive, S6K1 associates with the eIF3 complex, while the S6K1 activator mTOR/raptor does not.

S6K1 is an effector and a mediator of mTOR complex 1 (mTORC1) in regulating protein synthesis and integrating diverse signals into control of cell growth and response to stress. Here, we show that eIF3a regulates S6K1 activity by inhibiting mTORC1 kinase via regulating Raptor synthesis.

eIF3 family members as S6K1 interactors represented a potentially important connection between the mTOR pathway and an integral component of the translational preinitiation apparatus. After confirming the interaction between endogenous S6K1 and eIF3, the authors set upon uncovering poten-tial mechanisms that regulate this interaction. They

2005年12月9日 · In the November 18 issue of Cell, discover an unidentified function for the eIF3 translation initiation factor as a scaffold for the dynamic associations of many preinitiation complex components, including the growth-regulating kinases mTOR and S6K1.

2005年12月9日 · After confirming the interaction between endogenous S6K1 and eIF3, the authors set upon uncovering potential mechanisms that regulate this interaction. They found that multiple stimuli, including growth factors and nutrients, disrupt the association of S6K1, but not the related S6K2, with eIF3 in a rapamycin-sensitive fashion.

During terminal muscle differentiation a conserved TOS motif in eIF3f connects mTOR/raptor complex, which phosphorylates S6K1 and regulates downstream effectors of mTOR and Cap-dependent translation initiation. Thus eIF3f plays a major role for proper activity of mTORC1 to regulate skeletal muscle size.

2005年11月18日 · We show that mTOR and S6K1 maneuver on and off the eukaryotic initiation factor 3 (eIF3) translation initiation complex in a signal-dependent, choreographed fashion. When inactive, S6K1 associates with the eIF3 complex, while the S6K1 activator mTOR/raptor does not.