ArticleBiochemical and biophysical research communications2008
AMPK represses TOP mRNA translation but not global protein synthesis in liver.
Article in Biochemical and biophysical research communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Sertraline treatment prevents motor dysfunction in a Huntington's disease mouse model and functional decline in patients.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025Article
- Translation regulation in response to stress.The FEBS journal · 2024Review
- Does the blunted stimulation of skeletal muscle protein synthesis by aging in response to mechanical load result from impaired ribosome biogenesis?Frontiers in aging · 2023Review
- Glucagon-Dependent Suppression of mTORC1 is Associated with Upregulation of Hepatic FGF21 mRNA Translation.American journal of physiology. Endocrinology and metabolism · 2020Article
- The Psychiatric Risk Gene NT5C2 Regulates Adenosine Monophosphate-Activated Protein Kinase Signaling and Protein Translation in Human Neural Progenitor Cells.Biological psychiatry · 2019Article
- Article
- Identification of AMP-activated protein kinase targets by a consensus sequence search of the proteome.BMC systems biology · 2015Article
- Ribosome biogenesis: emerging evidence for a central role in the regulation of skeletal muscle mass.Journal of cellular physiology · 2014Review
- Emerging role of AMP-activated protein kinase in endocrine control of metabolism in the liver.Molecular and cellular endocrinology · 2013Review
- Tsc2, a positional candidate gene underlying a quantitative trait locus for hepatic steatosis.Journal of lipid research · 2012Article
- alpha-Lipoic acid increases energy expenditure by enhancing adenosine monophosphate-activated protein kinase-peroxisome proliferator-activated receptor-gamma coactivator-1alpha signaling in the skeletal muscle of aged mice.Metabolism: clinical and experimental · 2010Article
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
The AMP-activated protein kinase (AMPK) represses signaling through the mammalian target of rapamycin complex 1 (mTORC1). In muscle, repression of mTORC1 leads to a reduction in global protein synthesis. In contrast, repression of mTORC1 in the liver has no immediate effect on global protein synthesis. In the present study, signaling through mTORC1 and translation of specific mRNAs such as those bearing a 5'-terminal oligopyrimidine (TOP) tract and were examined in rat liver following activation of AMPK after treadmill running. Activation of AMPK repressed translation of the TOP mRNAs encoding rpS6, rpS8, and eEF1alpha. In contrast, neither global protein synthesis nor translation of mRNAs encoding GAPDH or beta-actin was changed. Basal phosphorylation of the mTORC1 target 4E-BP1, but not S6K1 or rpS6, was reduced following activation of AMPK. Thus, in liver, AMPK activation repressed translation of TOP mRNAs through a mechanism distinct from downregulated phosphorylation of S6K1 or rpS6.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.