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Literature summary for 1.2.4.1 extracted from

  • Wijenayake, S.; Luu, B.E.; Zhang, J.; Tessier, S.N.; Quintero-Galvis, J.F.; Gaitan-Espitia, J.D.; Nespolo, R.F.; Storey, K.B.
    Strategies of biochemical adaptation for hibernation in a South American marsupial, Dromiciops gliroides 4. Regulation of pyruvate dehydrogenase complex and metabolic fuel selection (2018), Comp. Biochem. Physiol. B, 224, 32-37 .
    View publication on PubMed
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Organism

Organism UniProt Comment Textmining
Dromiciops gliroides
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Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein enzyme is subject to regulation by phosphorylation at residues S232, S293, S300 Dromiciops gliroides

Source Tissue

Source Tissue Comment Organism Textmining
heart
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 Dromiciops gliroides
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kidney
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 Dromiciops gliroides
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liver
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 Dromiciops gliroides
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skeletal muscle
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 Dromiciops gliroides
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General Information

General Information Comment Organism
physiological function within the pyruvate dehydrogenase complex, the E1 enzyme pyruvate dehydrogenase (PDH) is the main regulatory site and is subject to inhibitory phosphorylation. Total PDH content does not change significantly during hibernation in any tissue but phospho-PDH content increases in all. Heart PDH shows increased phosphorylation at the three sites S232, S293, S300 by 8.1-, 10.6- and 2.1fold, respectively. Liver also shows elevated phospho-S300 (2.5fold) and phospho-S293 (4.7fold) content. Phosphorylation of S232 and S293 increases significantly in brain and lung but only S232 phosphorylation increases in kidney and skeletal muscle Dromiciops gliroides