Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10815713 | Cellular Signalling | 2011 | 8 Pages |
Abstract
Protein translation is an essential but energetically expensive process, which is carefully regulated in accordance to the cellular nutritional and energy status. Eukaryotic elongation factor 2 (eEF2) is a central regulation point since it mediates ribosomal translocation and can be inhibited by phosphorylation at Thr56. TRPM7 is the unique fusion of an ion channel with a functional Ser/Thr-kinase. While TRPM7's channel function has been implicated in regulating vertebrate Mg2+ uptake required for cell growth, the function of its kinase domain remains unclear. Here, we show that under conditions where cell growth is limited by Mg2+ availability, TRPM7 via its kinase mediates enhanced Thr56 phosphorylation of eEF2. TRPM7-kinase does not appear to directly phosphorylate eEF2, but rather to influence the amount of eEF2's cognate kinase eEF2-k, involving its phosphorylation at Ser77. These findings suggest that TRPM7's structural duality ensures ideal positioning of its kinase in close proximity to channel-mediated Mg2+ uptake, allowing for the adjustment of protein translational rates to the availability of Mg2+.
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Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Anne-Laure Perraud, Xiaoyun Zhao, Alexey G. Ryazanov, Carsten Schmitz,