Regulation of the CoA Biosynthetic Complex Assembly in Mammalian Cells
<p>Generation and analysis of HEK293 cell lines with stable overexpression of EE-tagged Pank1β using lentiviral expression system. (<b>A</b>) Schematic diagram of the coenzyme A (CoA) biosynthetic pathway in mammalian cells. (<b>B</b>) Western blot analysis of EE-Pank1β expression in parental (HEK293) and stable (HEK293/Pank1β) cell lines. Lane 1—HEK293 cells infected with pLex alone (HEK293/pLex); Lane 2—stable HEK293/Pank1β cell line generated by selection for puromycin resistance of cells infected with pLex/Pank1β; Lane 3—transient overexpression of Pank1β in parental HEK293 cells by transfection with pLex/Pank1β, used as positive control. Figure is representative of three independent experiments.</p> "> Figure 2
<p>Validation of the proximity ligation assay (PLA) on HEK293/Pank1β cells for the detection of proximity between Pank1 and other enzymes of the CoA biosynthetic pathway. The associations of Pank1 with CoAsy (<b>A</b>), PPCS (<b>B</b>) and PPCDC (<b>C</b>) are shown in exponentially growing HEK293/Pank1β cells. Nuclei stained with DAPI (blue); PLA performed for Pank1 and other enzymes of the CoA biosynthesis (Red). Scale bars: 15 μm. Data are representative of three independent experiments.</p> "> Figure 3
<p>Serum starvation and treatment of HEK293/Pank1β cells with hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>) induce the Pank1/CoAsy association in situ. (<b>A</b>) Pank1 interaction with CoAsy is significantly increased in HEK293/Pank1β cells in response to serum starvation (16 h) or serum starvation (16 h) followed by treatment with 500 μΜ H<sub>2</sub>O<sub>2</sub> (10 min). Nuclei are stained with DAPI (blue); proximity ligation assay (PLA) performed for Pank1 and CoAsy (Red). Scale bars: 15 μm. Images are representative of three independent experiments. (<b>B</b>) Relative quantitation of Pank1/CoAsy assembly in control untreated and 16 h serum-starved HEK293/Pank1β cells from (<b>A</b>). Dots/cell counted. Data are presented as mean ± standard error of the mean (SEM) from <span class="html-italic">n</span> = 3 experiments (* <span class="html-italic">p</span> < 0.05). (<b>C</b>) Relative quantification of the mean fluorescence intensity per cell for control untreated and serum starved + H<sub>2</sub>O<sub>2</sub> treated cells from (<b>A</b>). Data represent mean ± SEM from <span class="html-italic">n</span> = 3 experiments (** <span class="html-italic">p</span> < 0.01).</p> "> Figure 4
<p>Insulin treatment inhibits the interaction between Pank1 and CoAsy in serum-starved HEK293/Pank1β cells. (<b>A</b>) Pank1 and CoAsy interaction is inhibited in response to insulin treatment in HEK293/Pank1β cells. Cells were starved for 16 h and treated with 1 μΜ insulin for 3 h or 6 h. Control cells were not starved or treated with insulin. Nuclei are stained with DAPI (blue); proximity ligation assay (PLA) was performed for Pank1 and CoAsy (Red). Scale bars: 15 μm. Data are representative of three independent experiments. (<b>B</b>) Relative quantitation of Pank1/CoAsy association in tested conditions from (<b>A</b>). Dots/cell counted. Data are presented as mean ± standard error of the mean (SEM) from <span class="html-italic">n</span> = 3 experiments (* <span class="html-italic">p</span> < 0.05; ** <span class="html-italic">p</span> < 0.01; *** <span class="html-italic">p</span> < 0.001).</p> "> Figure 5
<p>Asociation between endogenous enzymes of the CoA biosynthetic pathway is induced in A549 cells in response to serum starvation and oxidative stress. (<b>A</b>,<b>D</b>,<b>G</b>) Pank1 interacts with CoAsy, PPCS and PPCDC in A549 cells in response to serum starvation for 24 h or serum starvation followed by 10 min treatment with 500 μΜ H<sub>2</sub>O<sub>2</sub>. Nuclei are stained with DAPI (blue); proximity ligation assay (PLA) was performed for Pank1 and other enzymes of the CoA biosynthesis (Red). PLA images are representative of three independent experiments. (<b>B</b>,<b>E</b>,<b>H</b>) Relative quantitation of fluorescent dots/cell of Pank1/CoAsy, Pank1/PPCS and Pank1/PPCDC assembly in control untreated and serum starved A549 cells from (<b>A</b>,<b>D</b>,<b>G</b>). Data are presented as mean ± standard error of the mean (SEM) from <span class="html-italic">n</span> = 3 experiments (*** <span class="html-italic">p</span> <0.001). (<b>C</b>,<b>F</b>,<b>I</b>) Relative quantification of the mean fluorescence intensity per cell of Pank1/CoAsy, Pank1/PPCS and Pank1/PPCDC for control untreated and serum starved + H<sub>2</sub>O<sub>2</sub> treated cells from (<b>A</b>,<b>D</b>,<b>G</b>). Data are presented as mean ± SEM from <span class="html-italic">n</span> = 3 experiments (*** <span class="html-italic">p</span> < 0.001).</p> "> Figure 6
<p>Insulin and fibroblast growth factor 2 (FGF-2) inhibit the interaction between Pank1 and CoAsy in A549 cells. Pank1 and CoAsy interaction is inhibited in response to insulin (<b>A</b>) and FGF-2 (<b>B</b>) treatment in A549 cells. Cells were starved for 24 h and treated with 1 μΜ insulin or 100 ng/mL FGF2 for 3 h or 6 h. Control cells were not starved or treated. Nuclei are stained with DAPI (blue); proximity ligation assay (PLA) was performed for Pank1 and CoAsy (Red). Scale bars: 15 μm. Data are representative of three independent experiments. (<b>C</b>,<b>D</b>) Relative quantitation of Pank1/CoAsy assembly in control, serum starved, and insulin or FGF-2 treated A549 cells from (<b>A</b>,<b>B</b>). Dots/cell counted. Data represent mean ± SEM from <span class="html-italic">n</span> = 3 experiments (*** <span class="html-italic">p</span> < 0.001).</p> "> Figure 7
<p>(<b>A</b>) Key players of the CoA biosynthetic pathway in bacteria, yeast and mammals. Solid rectangle indicates components of the CoA-synthesizing protein complex (CoA-SPC) described in yeast [<a href="#B18-ijms-22-01131" class="html-bibr">18</a>]. Dotted rectangle indicates a potential CoA biosynthetic complex (CoA-BC) in mammalian cells. (<b>B</b>) Negative and positive regulators of CoA biosynthesis in mammalian cells. Apart from the outer mitochondrial membrane (OMM), CoAsy was found to be localized in the mitochondrial matrix and nucleus [<a href="#B18-ijms-22-01131" class="html-bibr">18</a>,<a href="#B26-ijms-22-01131" class="html-bibr">26</a>,<a href="#B30-ijms-22-01131" class="html-bibr">30</a>,<a href="#B31-ijms-22-01131" class="html-bibr">31</a>].</p> ">
Abstract
:1. Introduction
2. Results
2.1. Analysis of the CoA Biosynthetic Complex in HEK293/Pank1β Cells Using Conventional Approaches
2.2. Validation of the Proximity Ligation Assay for Testing the Interaction between Enzymes of CoA Biosynthesis
2.3. Oxidative Stress and Serum Starvation Induce the Association of CoA Biosynthetic Enzymes
2.4. Treatment of Serum-Starved Cells with Insulin Promotes the Dissociation of CoA Biosynthetic Enzymes
2.5. Assembly of Endogenous CoA Biosynthetic Enzymes is Induced in A549 Cells in Response to Oxidative Stress
2.6. Growth Signaling Inhibits the Assembly of Endogenous CoA Biosynthetic Enzymes in A549 Cells
3. Discussion
4. Materials and Methods
4.1. Reagents and Chemicals
Antibodies
4.2. Cell Culture and Generation of the HEK293/Pank1β Cell Line
4.3. Treatment of HEK293/Pank1β and A549 Cells
4.4. SDS-PAGE and Western Blot Analysis
4.5. Proximity Ligation Assay
4.6. Statistical Analysis
Supplementary Materials
Author Contributions
Funding
Data Availability Statement
Conflicts of Interest
Abbreviations
CoA | Coenzyme A |
PanK | Pantothenate kinase |
PPCS | 4′-phosphopantothenoylcysteine synthetase |
PPCDC | 4′-phosphopantothenoylcysteine decarboxylase |
CoAsy | CoA synthase |
PLA | Proximity ligation assay |
FGF | Fibroblast growth factor |
NBIA | Neurodegeneration with brain iron accumulation |
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Baković, J.; López Martínez, D.; Nikolaou, S.; Yu, B.Y.K.; Tossounian, M.-A.; Tsuchiya, Y.; Thrasivoulou, C.; Filonenko, V.; Gout, I. Regulation of the CoA Biosynthetic Complex Assembly in Mammalian Cells. Int. J. Mol. Sci. 2021, 22, 1131. https://doi.org/10.3390/ijms22031131
Baković J, López Martínez D, Nikolaou S, Yu BYK, Tossounian M-A, Tsuchiya Y, Thrasivoulou C, Filonenko V, Gout I. Regulation of the CoA Biosynthetic Complex Assembly in Mammalian Cells. International Journal of Molecular Sciences. 2021; 22(3):1131. https://doi.org/10.3390/ijms22031131
Chicago/Turabian StyleBaković, Jovana, David López Martínez, Savvas Nikolaou, Bess Yi Kun Yu, Maria-Armineh Tossounian, Yugo Tsuchiya, Christopher Thrasivoulou, Valeriy Filonenko, and Ivan Gout. 2021. "Regulation of the CoA Biosynthetic Complex Assembly in Mammalian Cells" International Journal of Molecular Sciences 22, no. 3: 1131. https://doi.org/10.3390/ijms22031131