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M-LDH serves as a regulatory subunit of the cytosolic substrate-channelling complex in vivo.

Abstract：

:Nucleoside diphosphate kinase A (NDPK-A) regulates the alpha1 isoform of the AMP-activated protein kinase (AMPK alpha1) 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 alpha1 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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Jovanović S,Jovanović A,Crawford RM

doi

10.1016/j.jmb.2007.05.081

subject

Has Abstract

pub_date

2007-08-10 00:00:00

pages

349-61

issue

2

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(07)00742-5

journal_volume

371

pub_type

杂志文章

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