ArticleScientific reports2017
Global view of cognate kinase activation by the human pyruvate dehydrogenase complex.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Maternal slow-release nitrogen diets during late gestation optimize the energy metabolism in calves' skeletal muscle.PloS one · 2026Article
- Autoantibodies Against Dihydrolipoamide S-Acetyltransferase in Immune-Mediated Neuropathies.Neurology(R) neuroimmunology & neuroinflammation · 2024Article
- The structure and evolutionary diversity of the fungal E3-binding protein.Communications biology · 2023Article
- Impact of Maternal Feed Restriction at Different Stages of Gestation on the Proteomic Profile of the Newborn Skeletal Muscle.Animals : an open access journal from MDPI · 2022Article
- Development and validation of a novel diagnostic model for musculoskeletal aging (sarcopenia) based on cuproptosis-related genes associated with immunity.American journal of translational research · 2022Article
- Reversing tozasertib resistance in glioma through inhibition of pyruvate dehydrogenase kinases.Molecular oncology · 2022Article
- A multipronged approach unravels unprecedented protein-protein interactions in the human 2-oxoglutarate dehydrogenase multienzyme complex.The Journal of biological chemistry · 2018Article
- Defining the contribution of skeletal muscle pyruvate dehydrogenase α1 to exercise performance and insulin action.American journal of physiology. Endocrinology and metabolism · 2018Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The human pyruvate dehydrogenase complex (PDC) comprises four multidomain components, E1, E3, E2 and an E3-binding protein (E3BP), the latter two forming the core as E2·E3BP sub-complex. Pyruvate flux through PDC is regulated via phosphorylation (inactivation) at E1 by four PDC kinases (PDKs), and reactivation by two PDC phosphatases. Up-regulation of PDK isoform gene expression is reported in several forms of cancer, while PDKs may be further activated by PDC by binding to the E2·E3BP core. Hence, the PDK: E2·E3BP interaction provides new therapeutic targets. We carried out both functional kinetic and thermodynamic studies to demonstrate significant differences in the activation of PDK isoforms by binding to the E2·E3BP core: (i) PDK2 needs no activation by E2·E3BP for efficient functioning, while PDK4 was the least effective of the four isoforms, and could not be activated by E2·E3BP. Hence, development of inhibitors to the interaction of PDK2 and PDK4 with E2·E3BP is not promising; (ii) Design of inhibitors to interfere with interaction of E2·E3BP with PDK1 and PDK3 is promising. PDK3 needs E2·E3BP core for activation, an activation best achieved by synergistic combination of E2-derived catalytic domain and tridomain.
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