Phosphoprotein Analysis: From Proteins to Proteomes
Author Information
Author(s): Frédéric Delom, Eric Chevet
Primary Institution: McGill University
Hypothesis
Characterization of protein modification by phosphorylation is essential for understanding cellular processes.
Conclusion
The review discusses various methods for the enrichment, identification, quantitation, and validation of phosphoproteins and their phosphorylation sites.
Supporting Evidence
- Phosphorylation is a key reversible modification that regulates many protein functions.
- Mass spectrometry has emerged as a reliable method for characterizing protein phosphorylation sites.
- The stoichiometry of phosphorylation is generally low, making it challenging to analyze.
Takeaway
This study looks at how scientists can find and measure proteins that have been changed by adding phosphate groups, which is important for how cells work.
Methodology
The review surveys methods for identifying phosphoproteins and phosphopeptides, mapping phosphorylation sites, and quantifying and validating these events.
Limitations
Phosphoprotein analysis is complicated due to low abundance, variability in phosphorylation sites, and the need to inhibit phosphatase activity during sample preparation.
Digital Object Identifier (DOI)
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