Proteomics,Multiomics

Dataset Information

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


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 Ca2+/calmodulin-dependent protein kinase kinase β (CaMKKβ). In response, AMPK impinges on the autophagy regulators Unc-51-like kinase-1 (ULK1) and c-Jun. AMPK is widely recognized as an mTORC1 antagonist that is activated by starvation. We find that aa acutely activate AMPK concurrently with mTOR. We show that AMPK under aa sufficiency acts to sustain autophagy. This may be required to maintain protein homoeostasis and deliver metabolite intermediates for biosynthetic processes.

OTHER RELATED OMICS DATASETS IN: BIOMD0000000640

INSTRUMENT(S): LTQ Orbitrap XL

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Myoblast

SUBMITTER: Horvatovich Péter  

LAB HEAD: Kathrin Thedieck

PROVIDER: PXD003073 | Pride | 2016-12-12

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
20130830_JS_RT_AB0621_TIO_FR1.raw Raw
20130830_JS_RT_AB0621_TIO_FR10_2.raw Raw
20130830_JS_RT_AB0621_TIO_FR11.raw Raw
20130830_JS_RT_AB0621_TIO_FR12.raw Raw
20130830_JS_RT_AB0621_TIO_FR13.raw Raw
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Publications


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 (AM  ...[more]

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