Skip Navigation


Briefings in Functional Genomics and Proteomics Advance Access originally published online on February 7, 2006
Briefings in Functional Genomics and Proteomics 2006 4(4):363-376; doi:10.1093/bfgp/eli007
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
4/4/363    most recent
eli007v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Goshe, M. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Goshe, M. B.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions please email: journals.permissions@oxfordjournals.org

Technique Review

Characterizing phosphoproteins and phosphoproteomes using mass spectrometry

Michael B. Goshe

Dr Michael B. Goshe, Department of Molecular and Structural Biochemistry, North Carolina State University, 128 Polk Hall, Campus Box 7622, Raleigh, NC 27695-7622, USA. Tel: +1 919 513 7740; Fax: +1 919 515 2047; E-mail: michael_goshe{at}ncsu.edu

The reversible phosphorylation of proteins plays a major role in many vital cellular processes by modulating protein function and transmitting signals within cellular pathways and networks. Because phosphorylation is dynamic and the sites of modification cannot be predicted by an organism's genome, proteomic measurements are required to identify sites of and changes in the phosphorylation state of proteins. The low stoichiometry of phosphorylation sites that accompany the multifarious nature of protein phosphorylation in biological systems continues to challenge the dynamic range of present mass spectrometry (MS) technologies and proteomic measurements, despite the preponderance of research and analytical methods devoted to this area. This review addresses some of the strategies and limitations involving the use of MS to map and quantify changes in protein phosphorylation sites for samples that range from a single protein to an entire proteome, and presents several compelling reasons as to why comprehensive phosphorylation site analysis has proven to be so elusive without a hypothesis-driven experimental approach to elicit more meaningful and confident results.

Keywords: phosphoprotein, phosphoproteomics, proteomics, liquid chromatography, mass spectrometry, affinity labeling, stable isotope coding, quantification, quantitation


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Mol. Cell. ProteomicsHome page
T. F. Wu and D. S. Chu
Sperm Chromatin: Fertile Grounds for Proteomic Discovery of Clinical Tools
Mol. Cell. Proteomics, October 1, 2008; 7(10): 1876 - 1886.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Yu, N. Ge, M. Xie, W. Sun, S. Burlingame, A. K. Pass, J. G. Nuchtern, D. Zhang, S. Fu, M. D. Schneider, et al.
Phosphorylation of Thr-178 and Thr-184 in the TAK1 T-loop Is Required for Interleukin (IL)-1-mediated Optimal NF{kappa}B and AP-1 Activation as Well as IL-6 Gene Expression
J. Biol. Chem., September 5, 2008; 283(36): 24497 - 24505.
[Abstract] [Full Text] [PDF]

Home page
 Brief BioinformHome page
B.-J. M. Webb-Robertson and W. R. Cannon
Current trends in computational inference from mass spectrometry-based proteomics
Brief Bioinform, September 1, 2007; 8(5): 304 - 317.
[Abstract] [Full Text] [PDF]

Home page
 Brief Funct Genomic ProteomicHome page
K. J. Grant and C. C. Wu
Advances in neuromembrane proteomics: efforts towards a comprehensive analysis of membrane proteins in the brain
Brief Funct Genomic Proteomic, March 12, 2007; (2007) elm001v1.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.