Document Detail

Towards functional phosphoproteomics by mapping differential phosphorylation events in signaling networks.
MedLine Citation:
PMID:  18972525     Owner:  NLM     Status:  MEDLINE    
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.
Sergio de la Fuente van Bentem; Wieslawa I Mentzen; Alberto de la Fuente; Heribert Hirt
Related Documents :
19513205 - A novel two-component system bqss-bqsr modulates quorum sensing-dependent biofilm decay...
19303165 - Plastid signalling to the nucleus: messengers still lost in the mists?
23708135 - Carbohydrate kinase (rhak)-dependent abc transport of rhamnose in rhizobium leguminosar...
20057515 - Walkmycin b targets walk (yycg), a histidine kinase essential for bacterial cell growth.
3667615 - Stopped-flow studies of spectral changes in human serum albumin following an alkaline p...
19201855 - A kinase-dead allele of lyn attenuates autoimmune disease normally associated with lyn ...
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    
Department of Plant Molecular Biology, Max F. Perutz Laboratories, University of Vienna, Vienna, Austria.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Antineoplastic Agents / therapeutic use
Data Interpretation, Statistical
Drug Discovery
Mass Spectrometry
Neoplasms / drug therapy,  metabolism
Phosphoproteins / physiology*
Protein Kinases / metabolism
Proteome / metabolism
Proteomics / methods*
Signal Transduction
Systems Biology
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

Previous Document:  Evaluation of the utility of neutral-loss-dependent MS3 strategies in large-scale phosphorylation an...
Next Document:  Application of electron transfer dissociation (ETD) for the analysis of posttranslational modificati...