The interaction between AMPKβ2 and the PP1-targeting subunit R6 is dynamically regulated by intracellular glycogen content.

The Biochemical Journal
Yvonne OligschlaegerDietbert Neumann

Abstract

AMP-activated protein kinase (AMPK) is a metabolic stress-sensing kinase. We previously showed that glucose deprivation induces autophosphorylation of AMPKβ at Thr-148, which prevents the binding of AMPK to glycogen. Furthermore, in MIN6 cells, AMPKβ1 binds to R6 (PPP1R3D), a glycogen-targeting subunit of protein phosphatase type 1 (PP1), thereby regulating the glucose-induced inactivation of AMPK. In the present study, we further investigated the interaction of R6 with AMPKβ and the possible dependency on Thr-148 phosphorylation status. Yeast two-hybrid (Y2H) analyses and co-immunoprecipitation (IP) of the overexpressed proteins in human embryonic kidney (HEK) 293T) cells revealed that both AMPKβ1 and AMPK-β2 wild-type (WT) isoforms bind to R6. The AMPKβ-R6 interaction was stronger with the muscle-specific AMPKβ2-WT and required association with the substrate-binding motif of R6. When HEK293T cells or C2C12 myotubes were cultured in high-glucose medium, AMPKβ2-WT and R6 weakly interacted. In contrast, glycogen depletion significantly enhanced this protein interaction. Mutation of AMPKβ2 Thr-148 prevented the interaction with R6 irrespective of the intracellular glycogen content. Treatment with the AMPK activator oligomycin enh...Continue Reading

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Mar 21, 2015·The Journal of Biological Chemistry·Yvonne OligschlaegerDietbert Neumann

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Citations

May 2, 2018·Biological & Pharmaceutical Bulletin·Qi WangGuizhen Tian
Aug 25, 2016·Clinical Science·Pablo B Martínez de MorentinMiguel López
Jan 5, 2020·Molecular & Cellular Proteomics : MCP·Zhen ChenJunjie Chen
Jan 17, 2021·Molecular & Cellular Proteomics : MCP·Zhen ChenJunjie Chen

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