AMPK represses TOP mRNA translation but not global protein synthesis in liver

Ali K. Reiter, Douglas R. Bolster, Stephen J. Crozier, Scot R. Kimball, Leonard S. Jefferson

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


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 eEF1α. In contrast, neither global protein synthesis nor translation of mRNAs encoding GAPDH or β-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.

Original languageEnglish (US)
Pages (from-to)345-350
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Sep 19 2008

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'AMPK represses TOP mRNA translation but not global protein synthesis in liver'. Together they form a unique fingerprint.

Cite this