• Home
  • Search Results
  • A systems study reveals concurrent activation of AMPK and mTOR by amino acids.

A systems study reveals concurrent activation of AMPK and mTOR by amino acids.

Nature communications (2016-11-22)
Piero Dalle Pezze, Stefanie Ruf, Annika G Sonntag, Miriam Langelaar-Makkinje, Philip Hall, Alexander M Heberle, Patricia Razquin Navas, Karen van Eunen, Regine C Tölle, Jennifer J Schwarz, Heike Wiese, Bettina Warscheid, Jana Deitersen, Björn Stork, Erik Fäßler, Sascha Schäuble, Udo Hahn, Peter Horvatovich, Daryl P Shanley, Kathrin Thedieck
ABSTRACT

Amino acids (aa) are not only building blocks for proteins, but also signalling molecules, with the mammalian target of rapamycin complex 1 (mTORC1) acting as a key mediator. However, little is known about whether aa, independently of mTORC1, activate other kinases of the mTOR signalling network. To delineate aa-stimulated mTOR network dynamics, we here combine a computational-experimental approach with text mining-enhanced quantitative proteomics. We report that AMP-activated protein kinase (AMPK), phosphatidylinositide 3-kinase (PI3K) and mTOR complex 2 (mTORC2) are acutely activated by aa-readdition in an mTORC1-independent manner. AMPK activation by aa is mediated by Ca

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Phosphatase Inhibitor Cocktail 3, DMSO solution
Sigma-Aldrich
MEM Amino Acids (50x) solution, Without L-glutamine, liquid, sterile-filtered, BioReagent, suitable for cell culture
Sigma-Aldrich
Insulin from bovine pancreas, γ-irradiated, BioXtra, suitable for cell culture, potency: ≥20 units/mg (USP units), lyophilized powder
Sigma-Aldrich
RPMI 1640 Amino Acids Solution (50×), Without L-glutamine, sterile-filtered, BioReagent, suitable for cell culture
Sigma-Aldrich
MISSION® esiRNA, targeting human IRS1