New insights to master signaling switch identified using high throughput technology platform

The findings were recently published online in the scientific journal Molecular & Cellular Proteomics from The American Society of Biochemistry & Molecular Biology.

A great challenge in science today is identifying the structure, function and interactions of the proteins within our bodies. By unravelling the cascades of interactions that occur in cells between proteins, scientists may pinpoint where these processes fail in various diseases.

Calmodulin is present in all cells and found at higher levels in those that are growing rapidly. This protein controls the level of calcium in cells, which is fundamental to the processes of cell proliferation, learning and memory, growth and movement. When calmodulin interacts with other proteins, calcium levels increase within cells.
 
Dr David O’Connell, a senior postdoctoral researcher working with Conway Fellow, Professor Dolores Cahill used a human protein array system to identify up to 70 novel interactions where calmodulin bound tightly to other proteins. These interactions were then verified and validated using high throughput technology.

Commenting on the findings, Dr O’Connell said, “This technology provides us with a versatile tool to identify the primary targets of central signalling proteins that regulate large numbers of proteins across all cells of the body. It has significant advantages over other methods currently in use. Our results now provide a starting point to gain greater insight into calcium signalling in the brain”. 

O’Connell will now begin to collaborate with UCD Conway colleagues who have previously identified calmodulin interacting with proteins in the course of their research and are now intrigued at the prospect that the presence of the protein may actually point to the cell processes they are investigating being calcium dependent.

Science Foundation Ireland partially funded this project through a Walton Fellowship awarded to Professor Sara Linse, a protein structural chemist from Lund University, Sweden who collaborated on the project.