mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events

(Cell, Vol. 123, 569–580; November 18, 2005) We, the editors of Cell, were contacted by a concerned reader regarding a duplication in Figure 2 of the above paper. Dr. John Blenis, the corresponding author, determined that the error was introduced during revision of the manuscript. In preparing the final version of Figure 2B, the panel showing results for eIF3b was mislabeled as HA (S6K1) lysate. A different exposure of the eIF3b panels published in Figures 2C and 2D was then mistakenly used for eIF3b, resulting in the duplication. The authors no longer have access to the original data for the HA (S6K1) lysate published 16 years ago, and as a consequence, a Correction is not possible. Given the age of the paper and that the duplication does not compromise the conclusions of the paper, based on the information available to us at this time, we believe that no further action is warranted. mTOR and S6K1 Mediate Assembly of the Translation Preinitiation Complex through Dynamic Protein Interchange and Ordered Phosphorylation EventsHolz et al.CellNovember 18, 2005In BriefIn response to nutrients, energy sufficiency, hormones, and mitogenic agents, S6K1 phosphorylates several targets linked to translation. However, the molecular mechanisms whereby S6K1 is activated, encounters substrate, and contributes to translation initiation are poorly understood. 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. Full-Text PDF Open Archive