AMP-activated Protein Kinase Up-regulates Mitogen-activated Protein (MAP) Kinase-interacting Serine/Threonine Kinase 1a-dependent Phosphorylation of Eukaryotic Translation Initiation Factor 4E

Xiaoqing Zhu, Vivian Dahlmans, Ramon Thali, Christian Preisinger, Benoit Viollet, J. Willem Voncken, Dietbert Neumann*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

7 Citations (Web of Science)


AMP-activated protein kinase (AMPK) is a molecular energy sensor that acts to sustain cellular energy balance. Although AMPK is implicated in the regulation of a multitude of ATP-dependent cellular processes, exactly how these processes are controlled by AMPK as well as the identity of AMPK targets and pathways continues to evolve. Here we identify MAP kinase-interacting serine/threonine protein kinase 1a (MNK1a) as a novel AMPK target. Specifically, we show AMPK-dependent Ser(353) phosphorylation of the human MNK1a isoform in cell-free and cellular systems. We show that AMPK and MNK1a physically interact and that in vivo MNK1a-Ser(353) phosphorylation requires T-loop phosphorylation, in good agreement with a recently proposed structural regulatory model of MNK1a. Our data suggest a physiological role for MNK1a-Ser(353) phosphorylation in regulation of the MNK1a kinase, which correlates with increased eIF4E phosphorylation in vitro and in vivo.
Original languageEnglish
Pages (from-to)17020-17027
JournalJournal of Biological Chemistry
Issue number33
Publication statusPublished - Aug 2016


  • AMP-activated kinase (AMPK)
  • eukaryotic translation initiation factor 4E (eIF4E)
  • mitogen-activated protein kinase (MAPK)
  • post-translational modification (PTM)
  • protein phosphorylation
  • translation
  • MAP kinase-interacting serine
  • threonine protein kinase 1a (MNK1a)

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