Sunday, October 30, 2011

Phosphorylation: New and Improved Ways

This article talks about new ways to detect phosphorylation. First off, what is phosphorylation? It is the addition of a phosphate (PO43-) group to a protein or other organic molecule. Phosphorylation plays a significant role in a wide range of cellular processes. After years of research, scientists now know that the presence of a phosphate molecule (usually attached to threonine, serine, and tyrosine residues) can show the difference between health and disease. Protein kinases transfer phosphate groups from ATP to the serine, threonine, or tyrosine residues on protein peptide substrates, which directly affects the activity and function of the target. Through time, research has revealed how cells respond to insulin, and how cancer can develop when there is a mishap in phosphorylation. Other discoveries are showing that phosphorylation could be involved in mood disorders, diabetes, and Alzheimer’s disease.

Studying phosphorylated proteins is always a challenge. Nowadays, a popular method in viewing these proteins is the use of antibodies that specifically bind phosphorylated proteins. The availability of phospho-specific antibodies has opened the door for the improvement of traditional methods as well as the development of new immunoassay techniques. These antibodies can be used as investigation to detect phosphorylated proteins on a Western blot (adaptation of the Southern blot procedure, used to identify specific amino-acid sequences in proteins). The Western blot is the most common method used for assessing the phosphorylation state of a protein.

Assessing protein phosphorylation is often an essential component of the biologist's collection for understanding intracellular factors underlying cellular activities. Given the important role kinases play, it is critical for researchers to have quality tools for measuring protein phosphorylation. Each technique excels in different contexts, and scientists should have the knowledge to choose the method that best fits the experimental design.


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