Correction: The pyruvate dehydrogenase complex regulates mitophagic trafficking and protein phosphorylation
Panagiota Kolitsida, Vladimir Nolic, Jianwen Zhou, Michael Stumpe, Natalie M Niemi, Jörn Dengjel, Hagai Abeliovich
TL;DR
This paper shows how the pyruvate dehydrogenase complex (PDC) controls protein phosphorylation and mitophagy by regulating specific enzymes.
Contribution
The study reveals a novel mechanism where the PDC directly regulates a phosphatase and kinases through allosteric interactions.
Findings
PDC mutations impact matrix protein phosphorylation and mitophagic trafficking.
PDC regulates kinases and a phosphatase through direct allosteric interactions.
Abstract
Mutations in the PDC affect the phosphorylation and mitophagic trafficking of matrix proteins, through the novel regulation of associated kinases and a phosphatase. We suggest that this occurs by the direct allosteric regulation of the phosphatase and kinases by the PDC.
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Taxonomy
TopicsBiochemical Acid Research Studies · Amino Acid Enzymes and Metabolism · Biochemical and Molecular Research
Article: Kolitsida P, Nolic V, Zhou J, Stumpe M, Niemi NM, Dengjel J, Abeliovich H (2023 Jul 13) The pyruvate dehydrogenase complex regulates mitophagic trafficking and protein phosphorylation. Life Sci Alliance 6(9): e202302149. doi: 10.26508/lsa.202302149. PMID: 37442609.
The authors would like to correct an error in Fig 6. A minus sign appears instead of a plus sign for Aup1-HA in the fourth column of the figure, which renders the results meaningless. The corrected version of Fig 6 is now provided.
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