Proteomics Moves From Expression to Turnover

Update and Future Perspective

Mary K Doherty; Phillip D Whitfield


Expert Rev Proteomics. 2011;8(3):325-334. 

In This Article

Five-year View

Proteomics is advancing at a rapid pace. The need to be able to accurately quantify changes in the proteome is now seen as integral to any proteomics analysis. However, simply being able to monitor changes in the amount of a protein over time fails to provide information as to how the cell exerts this change in concentration. In order to gain a fully 'systems' approach to biological investigations, it must be possible to directly interrogate the dynamics of change, in this case protein turnover. The ability to accurately define the synthesis and degradation rates of hundreds and thousands of proteins on a global scale represents a remarkable step forward in our ability to probe the dynamic proteome. In addition, as these approaches become routine, the bioinformatic solutions to data handling are becoming more sophisticated. The inclusion of non-mass spectrometric methodologies is also important, and will take on an increasingly important role as we move to comprehensive analysis of the dynamics of cellular function. The methodology for determining the synthesis and degradation rates of large numbers of proteins simultaneously has now been established. It is now time to use these methodologies to understand how cells react to changing environmental stresses and interventions. This has particular applicability in disease states, where the protein synthesis and degradation machinery have been impaired. In addition, although this approach is becoming routine in cell culture, there are still few studies in intact animals. As the field progresses, these approaches will provide opportunities to investigate fundamental aspects of physiological and pathophysiological processes.


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