Quantitative mass spectrometry of posttranslational modifications: Keys to confidence

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Science Signaling  07 Apr 2015:
Vol. 8, Issue 371, pp. re5
DOI: 10.1126/scisignal.aaa6466

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In this short Review, with 2 tables, 2 figures, and 31 references, we highlight how mass spectrometry analysis can be used to quantitatively study the proteome. In particular, we describe challenges to analyzing posttranslational modifications of proteins, which serve to transduce information through signaling pathways that control cellular behavior. Because posttranslational modifications serve as the language of cellular regulation, this systems-level approach reveals insights not only into basic cellular biology but also into how aberrations in these events can lead to disease. However, to leverage proteomic mass spectrometry data, the results need to be reliable, reproducible, and accurate, but technical limitations and variations in methodologies can make comparing data sets challenging.


Posttranslational modifications (PTMs) of proteins represent an important level of cellular control. They participate in the efficient transduction of signals and form the basis of long-term cellular memory, allowing cells to adapt to a rapidly changing environment. More than 200 different PTMs have been described that affect many aspects of protein functions, and the importance of these modifications is evident from the number of diseases that arise from their deregulation. The proteome-wide analysis of certain PTMs, such as phosphorylation, acetylation, glycosylation, methylation, ubiquitination, and sumoylation, has become a standard procedure in many laboratories. We highlight and discuss some important aspects of systems-wide PTM analyses using mass spectrometry–based methods.

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