Related Experiment Video
Updated: May 2, 2026
12:23
Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer
Published on: August 2, 2018
13.8K
Sample preparation and analytical strategies for large-scale phosphoproteomics experiments.
Evgeny Kanshin1, Stephen Michnick, Pierre Thibault
1IRIC, Institute for Research in Immunology and Cancer, Université de Montréal, P.O. Box 6128, Station, Centre-ville, Montréal, Québec H3C 3J7, Canada.
Seminars in Cell & Developmental Biology
|June 12, 2012
Summary
Reversible protein phosphorylation is a key post-translational modification. This review details mass spectrometry methods for identifying phosphorylation sites and understanding their functional impact.
Area of Science:
- Biochemistry
- Molecular Biology
- Proteomics
Background:
- Reversible protein phosphorylation is a crucial post-translational modification regulating diverse protein functions.
- Advances in phosphopeptide enrichment and mass spectrometry enable large-scale phosphoproteomics.
- Understanding phosphorylation's functional significance requires data on stoichiometry and protein abundance.
Purpose of the Study:
- To review sample preparation methods for mass spectrometry-based phosphoproteomics.
- To present analytical strategies for profiling protein phosphorylation.
- To elucidate the regulation of protein function by phosphorylation.
Main Methods:
- Mass spectrometry-based phosphoproteomics.
- Phosphopeptide enrichment techniques.
- Analysis of phosphorylation stoichiometry and protein abundance.
Main Results:
- Identification of thousands of phosphorylation sites.
- Profiling of protein phosphorylation across various systems.
- Insights into the regulation of protein function by phosphorylation.
Conclusions:
- Mass spectrometry is a powerful tool for phosphoproteomics.
- Detailed analysis is needed to understand phosphorylation's functional roles.
- This review provides a framework for phosphoproteomic studies.
