作者: Lindsay D. Rogers , Leonard J. Foster
DOI: 10.1039/B905580K
关键词: Transcription factor 、 Phosphoproteomics 、 Phosphopeptide 、 Phosphorylation 、 Biochemistry 、 Proteomics 、 Computational biology 、 Palmitoylation 、 Biology 、 Protein phosphorylation 、 Signal transduction
摘要: Networks of protein–protein and protein–metabolite interactions are commonly found in biological systems where signals must be passed from one location or component within a cell to another, such as receptor on the plasma membrane transcription factor nucleus. Regulation networks, signal transduction pathways, is often achieved by transient, reversible modification components involved. Several types post-translational modifications proteins employed including ubiquitylation lysines palmitoylation cysteines, but far best appreciated apparently most important involves phosphorylation serine, threonine tyrosine residues. Whilst protein has long been recognized functionally important, low stoichiometry ultimately impeded global analyses (phosphoproteomics). Recent developments application metal oxide chromatography advanced mass spectrometric techniques have enabled phosphoproteomics move beyond mere proof-of-principle experiments, stage it can successfully address complex questions. Here we cover development phosphopeptide/protein analysis spectrometry various used enrich phosphopeptides/proteins. We also speculate future phosphoproteomic research, now that goal generating datasets realized.