Response to Comment on "A Dynamic Network Model of mTOR Signaling Reveals TSC-Independent mTORC2 Regulation"Pezze, P. D., Sonntag, A. G., Shanley, D. P. & Thedieck, K., 10-Jul-2012, In : Science signaling. 5, 232, 4 p., 4.
Research output: Contribution to journal › Letter › Academic › peer-review
We modeled the mammalian or mechanistic target of rapamycin (mTOR) network and proposed a previously unknown mode of activation of the mTOR-containing complex mTORC2 through a phosphoinositide 3-kinase-dependent, and tuberous sclerosis complex-independent mechanism. Manning questions the validity of using the phosphorylation of Ser(2481) of mTOR as a specific readout of mTORC2 activity and suggests an in vitro mTORC2 kinase assay as a more appropriate method to parameterize a dynamic mTOR model. We maintain that our computational-experimental approach in combination with careful selection of the readout and cell system is appropriate for studying mTORC2 regulation by insulin.
|Number of pages||4|
|Publication status||Published - 10-Jul-2012|
- RICH AKT SUBSTRATE, 40 KDA PRAS40, PROTEIN-KINASE, MAMMALIAN TARGET, COMPLEX 2, PHOSPHORYLATION, ACTIVATION, AKT/PKB, SURVIVAL, INSULIN