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Dihydroxyacetone phosphate signals glucose availability to mTORC1
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Journal Article
Dihydroxyacetone phosphate signals glucose availability to mTORC1
2020
Overview
The mechanistic target of rapamycin complex 1 (mTORC1) kinase regulates cell growth by setting the balance between anabolic and catabolic processes. To be active, mTORC1 requires the environmental presence of amino acids and glucose. While a mechanistic understanding of amino acid sensing by mTORC1 is emerging, how glucose activates mTORC1 remains mysterious. Here, we used metabolically engineered human cells lacking the canonical energy sensor AMP-activated protein kinase to identify glucose-derived metabolites required to activate mTORC1 independent of energetic stress. We show that mTORC1 senses a metabolite downstream of the aldolase and upstream of the GAPDH-catalysed steps of glycolysis and pinpoint dihydroxyacetone phosphate (DHAP) as the key molecule. In cells expressing a triose kinase, the synthesis of DHAP from DHA is sufficient to activate mTORC1 even in the absence of glucose. DHAP is a precursor for lipid synthesis, a process under the control of mTORC1, which provides a potential rationale for the sensing of DHAP by mTORC1.
Levels of the glycolytic intermediate metabolite dihydroxyacetone phosphate are shown to signal cellular glucose availability to the mTORC1 complex through an AMPK-independent route.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ AMP-activated protein kinase
/ AMP-Activated Protein Kinases - metabolism
/ Biomedical and Life Sciences
/ Dihydroxyacetone - metabolism
/ Dihydroxyacetone Phosphate - biosynthesis
/ Dihydroxyacetone Phosphate - physiology
/ Enzymes
/ Fructose-Bisphosphate Aldolase - metabolism
/ Glucose
/ Humans
/ Kinases
/ Lipid Metabolism - physiology
/ Phosphotransferases (Alcohol Group Acceptor) - metabolism
/ Proteins
