Phosphoproteome Analysis of Drosophila melanogaster Embryos

Bo Zhai, Judit Villén, Sean A. Beausoleil, Julian Mintseris and Steven P. Gygi*
Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115
J. Proteome Res., 2008, 7 (4), pp 1675–1682
DOI: 10.1021/pr700696a
Publication Date (Web): March 8, 2008
Copyright © 2008 American Chemical Society
* Corresponding author: Department of Cell Biology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115. Phone, (617) 432-3155 ; fax, (617) 432-1144; e-mail, steven_gygi@hms.harvard.edu.

Abstract

Abstract Image

Protein phosphorylation is a key regulatory event in most cellular processes and development. Mass spectrometry-based proteomics provides a framework for the large-scale identification and characterization of phosphorylation sites. Here, we used a well-established phosphopeptide enrichment and identification strategy including the combination of strong cation exchange chromatography, immobilized metal affinity chromatography, and high-accuracy mass spectrometry instrumentation to study phosphorylation in developing Drosophila embryos. In total, 13720 different phosphorylation sites were discovered from 2702 proteins with an estimated false-discovery rate (FDR) of 0.63% at the peptide level. Because of the large size of the data set, both novel and known phosphorylation motifs were extracted using the Motif-X algorithm, including those representative of potential ordered phosphorylation events.

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History

  • Published In Issue April 04, 2008
  • Article ASAPMarch 08, 2008
  • Received: October 29, 2007
    Accepted:  ,
    Revised:  ,

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