Publication

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 journalLetterAcademicpeer-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.

Original languageEnglish
Article number4
Number of pages4
JournalScience signaling
Volume5
Issue number232
Publication statusPublished - 10-Jul-2012
Externally publishedYes

    Keywords

  • RICH AKT SUBSTRATE, 40 KDA PRAS40, PROTEIN-KINASE, MAMMALIAN TARGET, COMPLEX 2, PHOSPHORYLATION, ACTIVATION, AKT/PKB, SURVIVAL, INSULIN

ID: 25169860