Targeted Quantification of Protein Phosphorylation and Its Contributions towards Mathematical Modeling of Signaling Pathways
Abstract
Post-translational modifications (PTMs) are key regulatory mechanisms that can control protein function. Of these, phosphorylation is the most common and widely studied. Because of its importance in regulating cell signaling, precise and accurate measurements of protein phosphorylation across wide dynamic ranges are crucial to understanding how signaling pathways function. Although immunological assays are commonly used to detect phosphoproteins, their lack of sensitivity, specificity, and selectivity often make them unreliable for quantitative measurements of complex biological samples. Recent advances in Mass Spectrometry (MS)-based targeted proteomics have made it a more useful approach than immunoassays for studying the dynamics of protein phosphorylation. Selected reaction monitoring (SRM)—also known as multiple reaction monitoring (MRM)—and parallel reaction monitoring (PRM) can quantify relative and absolute abundances of protein phosphorylation in multiplexed fashions targeting specific pathways. In addition, the refinement of these tools by enrichment and fractionation strategies has improved measurement of phosphorylation of low-abundance proteins. The quantitative data generated are particularly useful for building and parameterizing mathematical models of complex phospho-signaling pathways. Potentially, these models can provide a framework for linking analytical measurements of clinical samples to better diagnosis and treatment of disease.
- Authors:
-
[1];
[1];
[1];
[1];
[1]
- Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
- Publication Date:
- Research Org.:
- Pacific Northwest National Laboratory (PNNL), Richland, WA (United States)
- Sponsoring Org.:
- USDOE; National Institutes of Health (NIH)
- OSTI Identifier:
- 1959008
- Report Number(s):
- PNNL-SA-179947
Journal ID: ISSN 1420-3049
- Grant/Contract Number:
- AC05-76RL01830; U01 CA227544; U54 DA049116; U01 DK124020; P41 GM103493
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Molecules
- Additional Journal Information:
- Journal Volume: 28; Journal Issue: 3; Journal ID: ISSN 1420-3049
- Publisher:
- MDPI
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; targeted phosphoproteomics; LC-SRM; quantification; phosphorylation; signaling; mathematical modeling; cancer
Citation Formats
Dakup, Panshak P., Feng, Song, Shi, Tujin, Jacobs, Jon M., Wiley, H. Steven, and Qian, Wei-Jun. Targeted Quantification of Protein Phosphorylation and Its Contributions towards Mathematical Modeling of Signaling Pathways. United States: N. p., 2023.
Web. doi:10.3390/molecules28031143.
Dakup, Panshak P., Feng, Song, Shi, Tujin, Jacobs, Jon M., Wiley, H. Steven, & Qian, Wei-Jun. Targeted Quantification of Protein Phosphorylation and Its Contributions towards Mathematical Modeling of Signaling Pathways. United States. https://doi.org/10.3390/molecules28031143
Dakup, Panshak P., Feng, Song, Shi, Tujin, Jacobs, Jon M., Wiley, H. Steven, and Qian, Wei-Jun. Mon .
"Targeted Quantification of Protein Phosphorylation and Its Contributions towards Mathematical Modeling of Signaling Pathways". United States. https://doi.org/10.3390/molecules28031143. https://www.osti.gov/servlets/purl/1959008.
@article{osti_1959008,
title = {Targeted Quantification of Protein Phosphorylation and Its Contributions towards Mathematical Modeling of Signaling Pathways},
author = {Dakup, Panshak P. and Feng, Song and Shi, Tujin and Jacobs, Jon M. and Wiley, H. Steven and Qian, Wei-Jun},
abstractNote = {Post-translational modifications (PTMs) are key regulatory mechanisms that can control protein function. Of these, phosphorylation is the most common and widely studied. Because of its importance in regulating cell signaling, precise and accurate measurements of protein phosphorylation across wide dynamic ranges are crucial to understanding how signaling pathways function. Although immunological assays are commonly used to detect phosphoproteins, their lack of sensitivity, specificity, and selectivity often make them unreliable for quantitative measurements of complex biological samples. Recent advances in Mass Spectrometry (MS)-based targeted proteomics have made it a more useful approach than immunoassays for studying the dynamics of protein phosphorylation. Selected reaction monitoring (SRM)—also known as multiple reaction monitoring (MRM)—and parallel reaction monitoring (PRM) can quantify relative and absolute abundances of protein phosphorylation in multiplexed fashions targeting specific pathways. In addition, the refinement of these tools by enrichment and fractionation strategies has improved measurement of phosphorylation of low-abundance proteins. The quantitative data generated are particularly useful for building and parameterizing mathematical models of complex phospho-signaling pathways. Potentially, these models can provide a framework for linking analytical measurements of clinical samples to better diagnosis and treatment of disease.},
doi = {10.3390/molecules28031143},
journal = {Molecules},
number = 3,
volume = 28,
place = {United States},
year = {Mon Jan 23 00:00:00 EST 2023},
month = {Mon Jan 23 00:00:00 EST 2023}
}
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