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Important Clues of Current Phosphoproteomic Approaches for Clinical Research

Elena López, Juan López Pascual and Julia Sequí

Mass Spectrometry-based phosphoproteomics tools are critical to understand the structure and dynamics of signalling that engages and migrates through the entire proteome. Approaches such as affinity purification followed by Mass Spectrometry (MS) have been used to elucidate relevant biological questions in health and disease. Thousands of proteins interact via physical and chemical association. Certain proteins can covalently modify other proteins post-translationally. These post-translational modifications (PTMs) ultimately give rise to the emergent functions of cells in sequence, space and time.
Understanding the functions of phosphorylated proteins thus requires one to study proteomes as linked-systems rather than collections of individual protein molecules.
The interacting proteome or protein-network knowledge has recently received much attention, as networksystems (signalling pathways) are effective snapshots in time of the proteome as a whole. MS approaches are clearly essential, in spite of the difficulties of some low abundance proteins (e.g some kinases).