The researchers at the University of Liverpool have made a new discovery in the field of cell signaling.
Generally, the signaling in cell regulates cell growth and repair in humans. However, abnormal cell signaling can lead to many diseases, including cancer and neurodegeneration. Hence, detecting specific proteins that control cell signaling in healthy and disease states could help speed up the discovery of disease biomarkers and drug targets.
A team from the University's Department of Biochemistry led by Professor Claire Eyers has shown that the occurrence of protein modification (phosphorylation) in cell signaling is far more diverse and complex that which was thought previously. They have utilised the novel technique of new analytical workflow involving mass spectrometry.
The main regulator of protein function i.e. protein phosphorylation (involves the addition of phosphate groups to protein), and defining site-specific phosphorylation is important to understand basic and disease biology.
The research was mainly focused on phosphorylation of the amino acids serine, threonine, and tyrosine in vertebrates. However, evidence suggests that the critical aspects of cell biology were also regulated by the phosphorylation of other ‘non-canonical’ amino acids.
But, unfortunately, the standard methods of characterisation of protein phosphorylation are mostly unsuitable for the analysis of these novel types of non-canonical phosphorylation. And that's the reason why the complete landscape of human protein phosphorylation has until now, remained unexplored.
This research study focuses on a new phosphopeptide enrichment strategy, which allows identification of histidine, arginine, lysine, aspartate, glutamate, and cysteine phosphorylation sites on human proteins by mass spectrometry-based phosphoproteomics.
The researchers remarkably found out that the number of unique ‘non-canonical’ phosphorylation sites is almost one-third of the number of sites of phosphorylation observed on the well-studied serine, threonine and tyrosine residues.
