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Figure 2. The dependence of PKCa activity on Ca2+ concentration. The molar ratios of the lipid components of the vesicles used to activate the enzyme are shown. Ca2+ concentration was 200 mmol. SD calculated from 3 independent experiments. doi:10.1371/jou
Figure 2. Figure 2. The dependence of PKCa activity on Ca2+ concentration. The molar ratios of the lipid components of the vesicles used to activate the enzyme are shown. Ca2+ concentration was 200 mmol. SD calculated from 3 independent experiments. doi:10.1371/journal.pone.0069041.g002

Description

PKCα enzymatic activity is plotted as a function of calcium concentration, demonstrating how PIP2 reduces the calcium requirement for maximal kinase activation.

More Figures from This Paper

The crystal structure of the PKCα C2 domain bound to calcium, phosphatidylserine, and PIP2 in a quaternary complex is rendered, showing the spatial arrangement of lipid-binding sites.

Figure 1

The crystal structure of the PKCα C2 domain bound to calcium, phosphatidylserine, and PIP2 in a quaternary complex is rendered, showing the spatial arrangement of lipid-binding sites.

diagram
The dependence of PKCα activity on phosphatidylserine (POPS) concentration in lipid vesicles reveals that PIP2 lowers the threshold of phosphatidylserine needed for enzyme activation.

Figure 3

The dependence of PKCα activity on phosphatidylserine (POPS) concentration in lipid vesicles reveals that PIP2 lowers the threshold of phosphatidylserine needed for enzyme activation.

chart
PKCα activity is shown as a function of diacylglycerol (DOG) molar percentage in lipid vesicles, illustrating the cofactor requirements for kinase activation.

Figure 4

PKCα activity is shown as a function of diacylglycerol (DOG) molar percentage in lipid vesicles, illustrating the cofactor requirements for kinase activation.

chart
The relationship between PIP2 concentration and PKCα activity demonstrates that increasing PIP2 in lipid vesicles progressively enhances kinase activation efficiency.

Figure 5

The relationship between PIP2 concentration and PKCα activity demonstrates that increasing PIP2 in lipid vesicles progressively enhances kinase activation efficiency.

chart

Figure 2

Chart
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Source Paper

Phosphatidylinositol 4,5-bisphosphate decreases the concentration of Ca2+, phosphatidylserine and diacylglycerol required for protein kinase C α to reach maximum activity.

PloS one (2013)

PMID: 23874859

DOI: 10.1371/journal.pone.0069041

Cite This Figure

![Figure 2: PKCα enzymatic activity is plotted as a function of calcium concentration, demonstrating how PIP2 reduces the calcium requirement for maximal kinase activation.](https://pdfs.citedhealth.com/figures/23874859/85.png)

> Source: Antonio L Egea-Jiménez et al. "Phosphatidylinositol 4,5-bisphosphate decreases the concentration of Ca2+, phosp." *PloS one*, 2013. PMID: [23874859](https://pubmed.ncbi.nlm.nih.gov/23874859/)
<figure>
  <img src="https://pdfs.citedhealth.com/figures/23874859/85.png" alt="PKCα enzymatic activity is plotted as a function of calcium concentration, demonstrating how PIP2 reduces the calcium requirement for maximal kinase activation." />
  <figcaption>Figure 2. PKCα enzymatic activity is plotted as a function of calcium concentration, demonstrating how PIP2 reduces the calcium requirement for maximal kinase activation.<br>  Source: Antonio L Egea-Jiménez et al. "Phosphatidylinositol 4,5-bisphosphate decreases the concentration of Ca2+, phosp." <em>PloS one</em>, 2013. PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/23874859/">23874859</a></figcaption>
</figure>

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