Protein–Protein Interactions and Quantitative Phosphoproteomic Analysis Reveal Potential Mitochondrial Substrates of Protein Phosphatase 2A-B’ζ Holoenzyme
Abstract
:1. Introduction
2. Methodology
2.1. Plant Material and Growth Conditions
2.2. Gene Cloning for in Planta Expression In Vivo
2.3. Sugar Dependence Assay
2.4. Quantitative Phosphoproteomics
2.5. Liquid Chromatography-Tandem Mass Spectrometry (LC-MS/MS)
2.6. Bioinformatics
3. Results and Discussion
3.1. Sugar Dependence Assay Points to a Role in Energy Metabolism
3.2. Selected B’ζ Putative Interactors Carry Ser and Thr Phosphorylation Sites
3.3. Verification of B’ζ Putative Interactors Involved in Energy Flow to Mitochondria
3.4. Additional Metabolic Enzymes Revealed by Phosphoproteomics
4. Conclusions
Supplementary Materials
Author Contributions
Funding
Data Availability Statement
Conflicts of Interest
References
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Elshobaky, A.; Lillo, C.; Hodén, K.P.; Kataya, A.R.A. Protein–Protein Interactions and Quantitative Phosphoproteomic Analysis Reveal Potential Mitochondrial Substrates of Protein Phosphatase 2A-B’ζ Holoenzyme. Plants 2023, 12, 2586. https://doi.org/10.3390/plants12132586
Elshobaky A, Lillo C, Hodén KP, Kataya ARA. Protein–Protein Interactions and Quantitative Phosphoproteomic Analysis Reveal Potential Mitochondrial Substrates of Protein Phosphatase 2A-B’ζ Holoenzyme. Plants. 2023; 12(13):2586. https://doi.org/10.3390/plants12132586
Chicago/Turabian StyleElshobaky, Ahmed, Cathrine Lillo, Kristian Persson Hodén, and Amr R. A. Kataya. 2023. "Protein–Protein Interactions and Quantitative Phosphoproteomic Analysis Reveal Potential Mitochondrial Substrates of Protein Phosphatase 2A-B’ζ Holoenzyme" Plants 12, no. 13: 2586. https://doi.org/10.3390/plants12132586