Insight into the Interactome of Intramitochondrial PKA Using Biotinylation-Proximity Labeling.

ABSTRACT: Mitochondria are fully integrated in cell signaling. Reversible phosphorylation is involved in adjusting mitochondrial physiology to the cellular needs. Protein kinase A (PKA) phosphorylates several substrates present at the external surface of mitochondria to maintain cellular homeostasis. However, few targets of PKA located inside the organelle are known. The aim of this work was to characterize the impact and the interactome of PKA located inside mitochondria. Our results show that the overexpression of intramitochondrial PKA decreases cellular respiration and increases superoxide levels. Using proximity-dependent biotinylation, followed by LC-MS/MS analysis and in silico phospho-site prediction, we identified 21 mitochondrial proteins potentially targeted by PKA. We confirmed the inter

SUBMITTER: Ould Amer Y 

PROVIDER: S-EPMC7663848 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature