Abstract
A comparison of phosphoproteomics datasets of six eukaryotes shows significant overlap between phosphoproteomes.
Highlights
Reversible phosphorylation of proteins is involved in a wide range of processes, ranging from signaling cascades to regulation of protein complex assembly
Recent developments in high-throughput phosphoproteomics studies have resulted in the availability of phosphopeptide datasets for many model organisms
In order to amend these datasets for comparative analysis, we imposed a relatively strict set of cutoffs on phosphopeptide calls in order to improve the uniformity and reduce noise caused by differences in scoring methods and thresholds
Summary
Reversible phosphorylation of proteins is involved in a wide range of processes, ranging from signaling cascades to regulation of protein complex assembly. Tools for the comparison of phosphoproteomes are emerging [4] These high-throughput datasets do not capture all phosphorylated peptides of a species under a given condition, large advances in enrichment strategies and mass spectrometry techniques have been made in the past few years, and studies comparing partial phosphoproteomes are emerging [5]. Even though both the incomprehensive nature of the data as well as differences in experimental procedures complicate comparative analysis, we can start to exploit these data. Comparative analysis of phosphoproteomics data could increase our understanding of phosphorylation and the evolution of the phosphorylation network as a systems level property
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