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Wiley Interdiscip Rev Syst Biol Med. 2010 May-Jun;2(3):255-276. doi: 10.1002/wsbm.41.


Ozlu N1,2, Akten B1,3,4, Timm W1,5,6, Haseley N1,7, Steen H1,5,6, Steen JAJ1,3,4.

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Proteomics Center at Children's Hospital Boston, Boston, MA, USA.
Department of Systems Biology, Harvard Medical School, 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.
Department of Pathology, Harvard Medical School, Boston, MA, USA.
Department of Pathology, Children's Hospital Boston, Boston, MA, USA.
Department of Biological Sciences, Rochester Institute of Technology, Rochester, NY, USA.


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.

[Indexed for MEDLINE]

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