Abstract
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 language | English |
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Pages (from-to) | 17020-17027 |
Journal | Journal of Biological Chemistry |
Volume | 291 |
Issue number | 33 |
DOIs | |
Publication status | Published - Aug 2016 |
Keywords
- 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)