# Correction: The pyruvate dehydrogenase complex regulates mitophagic trafficking and protein phosphorylation

**Authors:** Panagiota Kolitsida, Vladimir Nolic, Jianwen Zhou, Michael Stumpe, Natalie M Niemi, Jörn Dengjel, Hagai Abeliovich

PMC · DOI: 10.26508/lsa.202402684 · Life Science Alliance · 2024-03-14

## 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.

## Key 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.

## Full-text entities

- **Genes:** AUP1 (AUP1 lipid droplet regulating VLDL assembly factor) [NCBI Gene 550], PDC (phosducin) [NCBI Gene 5132] {aka MEKA, PHD, PhLOP, PhLP}

## Full text

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## Figures

1 figure with captions in the complete paper: https://tomesphere.com/paper/PMC10940167/full.md

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Source: https://tomesphere.com/paper/PMC10940167