Revealing Secrets of Cellular Phosphorylation Systems Using Mass Spectrometry

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Protein phosphorylation is a chemical modification utilized by all living organisms to alter the function of proteins and controls processes such as cellular communication, growth, metabolism, differentiation, and survival. The enzymes that add and remove phosphate molecules to proteins are called kinases and phosphatases respectively.  Since a delicate balance of reversible phosphorylation is essential for cellular homeostasis, the actions of all kinases/phosphatases are under tight surveillance. One of the most powerful analytical tools to study phosphorylation systems is biological mass spectrometry. Mass spectrometry based methods can rapidly identify functional multiprotein complexes containing kinases and phosphatases as well as directly map the location of phosphate addition to better study the consequence of the protein modification. Accordingly, the long term goal of our research program is to integrate mass spectrometry, biochemistry, and cell biology techniques to decipher the mechanistic details regulating poorly understood kinases and phosphatases predicted to regulate fundamental cellular processes.