Work

Phosphoproteome Analysis of Drosophila melanogaster Embryos

Year: 2008

Type: article

Abstract: 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, 13,720 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.

Source: Journal of Proteome Research

DOI: 10.1021/pr700696a

Authors: Bo Zhai, Judit Villén, Sean A. Beausoleil, Julian Mintseris, Steven P. Gygi

Institution: Harvard University

Language: Hebrew

Topic: Advanced Proteomics Techniques and Applications

Subfield: Spectroscopy

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funder: National Human Genome Research Institute

Awards: G538058837, The Protein Complex Map of the Drosophila Proteome, New Technologies for Quantitative Phosphorylation Analysis, G8868506658