Document Detail


Towards functional phosphoproteomics by mapping differential phosphorylation events in signaling networks.
MedLine Citation:
PMID:  18972525     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Protein phosphorylation plays a central role in many signal transduction pathways that mediate biological processes. Novel quantitative mass spectrometry-based methods have recently revealed phosphorylation dynamics in animals, yeast, and plants. These methods are important for our understanding of how differential phosphorylation participates in translating distinct signals into proper physiological responses, and shifted research towards screening for potential cancer therapies and in-depth analysis of phosphoproteomes. In this review, we aim to describe current progress in quantitative phosphoproteomics. This emerging field has changed numerous static pathways into dynamic signaling networks, and revealed protein kinase networks that underlie adaptation to environmental stimuli. Mass spectrometry enables high-throughput and high-quality analysis of differential phosphorylation at a site-specific level. Although determination of differential phosphorylation between treatments is analogous to detecting differential gene expression, the large body of statistical techniques that has been developed for analysis of differential gene expression is not generally applied for detecting differential phosphorylation. We suggest possible improvements for analysis of quantitative phosphorylation by increasing the number of biological replicates and adapting statistical tests used for gene expression profiling and widely implemented in freely available software tools.
Authors:
Sergio de la Fuente van Bentem; Wieslawa I Mentzen; Alberto de la Fuente; Heribert Hirt
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Publication Detail:
Type:  Journal Article; Review    
Journal Detail:
Title:  Proteomics     Volume:  8     ISSN:  1615-9861     ISO Abbreviation:  Proteomics     Publication Date:  2008 Nov 
Date Detail:
Created Date:  2008-11-04     Completed Date:  2008-12-10     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  101092707     Medline TA:  Proteomics     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  4453-65     Citation Subset:  IM    
Affiliation:
Department of Plant Molecular Biology, Max F. Perutz Laboratories, University of Vienna, Vienna, Austria.
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MeSH Terms
Descriptor/Qualifier:
Animals
Antineoplastic Agents / therapeutic use
Data Interpretation, Statistical
Drug Discovery
Humans
Mass Spectrometry
Neoplasms / drug therapy,  metabolism
Phosphoproteins / physiology*
Phosphorylation
Protein Kinases / metabolism
Proteome / metabolism
Proteomics / methods*
Signal Transduction
Systems Biology
Chemical
Reg. No./Substance:
0/Antineoplastic Agents; 0/Phosphoproteins; 0/Proteome; EC 2.7.-/Protein Kinases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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