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Updated: Feb 3, 2026

Live-imaging of PKC Translocation in Sf9 Cells and in Aplysia Sensory Neurons
Published on: April 6, 2011
The story of PKC: A discovery marked by unexpected twists and turns
1Biosignal Research Center, Kobe University, Kobe, Japan.
Abstract:
Protein kinase C (PKC) is activated by 1,2-diacylglycerol as a second messenger in the signaling mechanism coupled with the hydrolysis of membrane inositol phospholipids, although it was not found by screening for a 1,2-diacylglycerol-dependent enzyme. PKC is also a receptor for the tumor-promoting phorbol esters, but it was not identified by its property of binding phorbol esters, either. Instead, the discovery and characterization of PKC, now known to comprise a family with multiple isoforms, was through a circuitous voyage filled with unexpected twists and turns. This review summarizes the discovery and the initial experiments of PKC as a historical perspective of the enzyme family in the context of the progress in the studies on protein phosphorylation. © 2018 IUBMB Life, 71(6):697-705, 2019.
Insights
Protein kinase C (PKC) is a family of enzymes crucial for cell signaling. Its discovery involved a complex, indirect path, not initially identified by its known activators like diacylglycerol or phorbol esters.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Signaling
Background:
- Protein kinase C (PKC) plays a vital role in cellular signal transduction pathways.
- PKC activation is linked to the hydrolysis of membrane inositol phospholipids and acts as a receptor for phorbol esters.
Purpose of the Study:
- To provide a historical perspective on the discovery and characterization of Protein Kinase C (PKC).
- To contextualize the enzyme family's emergence within the broader progress of protein phosphorylation research.
Main Methods:
- Review of historical scientific literature and initial experimental findings.
- Analysis of the indirect discovery process of PKC, highlighting unexpected findings.
Main Results:
- PKC was not initially identified through screening for 1,2-diacylglycerol-dependent enzymes or by its phorbol ester binding properties.
- The characterization of PKC, now recognized as a multi-isoform family, resulted from a complex and indirect scientific journey.
Conclusions:
- The discovery of PKC exemplifies the often non-linear progression of scientific research.
- Understanding the historical context of PKC discovery provides insight into the evolution of protein phosphorylation studies.
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