title: Phosphoproteomics.
abstract: Current analytical protein methods show phosphorylation to be the most ubiquitous, evolutionary conserved post-translational modification Post-Translational Modification (PTM). The reversible and transient nature of protein phosphorylation allows signal transduction pathways to carry out diverse cellular functions. From bacteria to humans, phosphorylation serves to modify protein function by altering protein stability, cellular location, substrate affinity, complex formation, and activity; thus allowing essential events such as cell cycle and growth to occur at precise times and locations. Phosphorylation controls a variety of events at many biological levels including: housekeeping activities controlled by single cells such as DNA transcription, cell-cycle regulation, and energy metabolism; and cellular processes that involve signaling between cells or the environment including such as neuronal migration and immune system recognition. This review summarizes state-of-the-art proteomics technologies available to study phosphorylation in biological systems. We highlight the tremendous steps the field has made in the last 5 years which allow quantitative global analyses while pointing out caveats in experimentation.
authors.affiliation: Proteomics Center at Children's Hospital Boston, Boston, MA, USA.|Department of Systems Biology, Harvard Medical School, Boston, MA, USA.
authors.forename: Nurhan
authors.initials: N
authors.lastname: Ozlu
authors.affiliation: Proteomics Center at Children's Hospital Boston, Boston, MA, USA.|F.M. Kirby Neurobiology Center, Children's Hospital Boston, Boston, MA 02115, USA.|Department of Neurobiology, Harvard Medical School, Boston, MA, USA.
authors.forename: Bikem
authors.initials: B
authors.lastname: Akten
authors.affiliation: Proteomics Center at Children's Hospital Boston, Boston, MA, USA.|Department of Pathology, Harvard Medical School, Boston, MA, USA.|Department of Pathology, Children's Hospital Boston, Boston, MA, USA.
authors.forename: Wiebke
authors.initials: W
authors.lastname: Timm
authors.affiliation: Proteomics Center at Children's Hospital Boston, Boston, MA, USA.|Department of Biological Sciences, Rochester Institute of Technology, Rochester, NY, USA.
authors.forename: Nathan
authors.initials: N
authors.lastname: Haseley
authors.affiliation: Proteomics Center at Children's Hospital Boston, Boston, MA, USA.|Department of Pathology, Harvard Medical School, Boston, MA, USA.|Department of Pathology, Children's Hospital Boston, Boston, MA, USA.
authors.forename: Hanno
authors.initials: H
authors.lastname: Steen
authors.affiliation: Proteomics Center at Children's Hospital Boston, Boston, MA, USA.|F.M. Kirby Neurobiology Center, Children's Hospital Boston, Boston, MA 02115, USA.|Department of Neurobiology, Harvard Medical School, Boston, MA, USA.
authors.forename: Judith A J
authors.initials: JAJ
authors.lastname: Steen
mesh_terms: D000818:Animals; D006801:Humans; D055442:Metabolome / Q000502:physiology*; D008954:Models, Biological; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation / Q000502:physiology*; D020543:Proteome / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*
chemical_list: D010750:Phosphoproteins; D020543:Proteome