Abstract
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).
Highlights
The word of proteomics is defined as the comprehensive analysis of the proteins which are expressed in cells or tissues, and can be employed at different stages
Using IMAC (Fe3+) and (TiO2) [26], the negatively charged phosphopeptides are purified by their affinity to positively charged metal ions, but some of these methods suffer the problem of binding acidic, non-phosphorylated peptides
Electron transfer dissociation (ETD) and electron capture dissociation (ECD) have shown great promise since the phosphate group remains attached during and after activationMany detected phosphopeptides contain multiple Ser/Thr/Tyr residues representing the likely possibility that there is more than one possible location for the site of phosphorylation within the peptide
Summary
The word of proteomics is defined as the comprehensive analysis of the proteins which are expressed in cells or tissues, and can be employed at different stages (e.g. healthy vs. disease). Important improvements are helping to achieve relevant data of phosphorylated kinases -being those proteins the “key” of signalling pathways and network-connectivity among different signalling cascades.
Sign-in/Register to view highlights & summary 
Published Version (
Free)
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call