Protein Phosphorylation and Cell Signaling Series II

Dear Colleagues,

Phosphorylation is one of the most important and most commonly occurring posttranslational modifications of proteins. Protein phosphorylation plays a critical role in cell signaling in response to extracellular stimulus and is of fundamental importance in biological regulation.

Protein phosphorylation is controlled by protein kinases and protein phosphatases. A protein kinase is a kinase enzyme that modifies other molecules, mostly proteins, by chemically adding phosphate groups to them (phosphorylation). The human genome contains about 518 protein kinase genes, and they constitute about 2% of all human genes. A protein could be phosphorylated in three amino acids, including tyrosine (Tyr, Y), Serine (Ser, S), and Threonine (Thr, T). A protein phosphatase is a phosphatase enzyme that removes a phosphate group from the phosphorylated amino acid residue of its substrate protein. While there are 107 genes in the human genome that encode protein tyrosine phosphatase, there are only a few serine/threonine phosphatases.

Up to 30% of all human proteins may be modified by protein kinase and phosphatase. Phosphorylation and de-phosphorylation commonly act as a switch to turn on and off a signaling cascade. Protein phosphorylation usually results in a functional change of the target protein (substrate) by changing enzyme activity, cellular location, or association with other proteins, which frequently lead to the changes in the biological function of the cell.

This Special Issue will cover the recent progress in all of the areas related to protein phosphorylation and cell signaling. Both original research articles and reviews are welcome.

Prof. Zhixiang Wang
Guest Editor

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