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• W2022973800 endingPage "361" @default.
• W2022973800 startingPage "349" @default.
• W2022973800 abstract "Nucleoside diphosphate kinase A (NDPK-A) regulates the α1 isoform of the AMP-activated protein kinase (AMPK α1) selectively, independent of [AMP] and surrounding [ATP], by a process termed substrate channelling. Here, we show, using a range of empirically validated biochemical techniques, that the muscle form (M-LDH or LDH-A) and the heart form (H-LDH or LDH-B) of lactate dehydrogenase are physically associated with the liver cytosolic substrate-channelling complex such that M-LDH associates with NDPK-A, AMPK α1 and casein kinase 2 (CK2), whereas H-LDH associates with local NDPK-B. We find that the species of LDH bound to the substrate-channelling complex regulates the in vivo enzymatic activities of both AMPK and CK2, and has a downstream effect on the phospho-status of acetyl CoA carboxylase, a key regulator of cellular fat metabolism known to be a part of the cytosolic substrate-channelling complex in vivo. We hypothesise that the regulatory presence of LDH in the complex couples the substrate-channelling mechanism to both the glycolytic and redox states of the cell, allowing for efficient sensing of cell metabolic status, interfacing with the substrate-channelling complex and regulating the enzymatic activities of AMPK and CK2, two critical protein kinases." @default.
• W2022973800 created "2016-06-24" @default.
• W2022973800 creator A5005135256 @default.
• W2022973800 creator A5062857959 @default.
• W2022973800 creator A5083580077 @default.
• W2022973800 date "2007-08-01" @default.
• W2022973800 modified "2023-09-27" @default.
• W2022973800 title "M-LDH Serves as a Regulatory Subunit of the Cytosolic Substrate-channelling Complex in Vivo" @default.
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• W2022973800 doi "https://doi.org/10.1016/j.jmb.2007.05.081" @default.
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