Phospho-proteomic analysis of cellular signaling

被引:37
作者
de Graauw, Marjo
Hensbergen, Paul
van de Water, Bob
机构
[1] Leiden Univ, Gorlaeus Labs, Div Toxicol, Leiden Amsterdam Ctr Drug Res, NL-2300 RA Leiden, Netherlands
[2] Leiden Univ, Med Ctr, Dept Parasitol, Biomol Mass Spectrometry Unit, Leiden, Netherlands
关键词
cellular signaling; phospho-proteomics; phosphorylation; signal transduction; tyrosine;
D O I
10.1002/elps.200600018
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Reversible protein phosphorylation plays an important role in the regulation of many different processes, such as cell growth, differentiation, migration, metabolism, and apoptosis. Identification of differentially phosphorylated proteins by means of phospho-proteomic analysis provides insight into signal transduction pathways that are activated in response to, for example, growth factor stimulation or toxicant-induced apoptosis. This review summarizes recent advances made in the field of phospho-proteomics and provides examples of how phospho-proteomic techniques can be combined to quantitatively investigate the dynamic changes in protein phosphorylation in time. By linking experimental data to clinical data (e.g., disease progression or response to therapy) new disease markers could be identified, which could then be validated for applications in disease diagnosis and progression or prediction of a response to drugs.
引用
收藏
页码:2676 / 2686
页数:11
相关论文
共 66 条
[1]   Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics [J].
Blagoev, B ;
Ong, SE ;
Kratchmarova, I ;
Mann, M .
NATURE BIOTECHNOLOGY, 2004, 22 (09) :1139-1145
[2]   A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling [J].
Blagoev, B ;
Kratchmarova, I ;
Ong, SE ;
Nielsen, M ;
Foster, LJ ;
Mann, M .
NATURE BIOTECHNOLOGY, 2003, 21 (03) :315-318
[3]   Quantitation of changes in protein phosphorylation: A simple method based on stable isotope labeling and mass spectrometry [J].
Bonenfant, D ;
Schmelzle, T ;
Jacinto, E ;
Crespo, JL ;
Mini, T ;
Hall, MN ;
Jenoe, P .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (03) :880-885
[4]   Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry [J].
Brill, LM ;
Salomon, AR ;
Ficarro, SB ;
Mukherji, M ;
Stettler-Gill, M ;
Peters, EC .
ANALYTICAL CHEMISTRY, 2004, 76 (10) :2763-2772
[5]  
BURNETT G, 1954, J BIOL CHEM, V211, P969
[6]   PROTEIN-KINASE ACTIVITY ASSOCIATED WITH AVIAN-SARCOMA VIRUS SRC GENE PRODUCT [J].
COLLETT, MS ;
ERIKSON, RL .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1978, 75 (04) :2021-2024
[7]  
COLLINS MO, 2005, SCI STKE 200K, pI6
[8]   An enriched look at tyrosine phosphorylation [J].
Conrads, TP ;
Veenstra, TD .
NATURE BIOTECHNOLOGY, 2005, 23 (01) :36-37
[9]   Kinome profiling for studying lipopolysaccharide signal transduction in human peripheral blood mononuclear cells [J].
Diks, SH ;
Kok, K ;
O'Toole, T ;
Hommes, DW ;
van Dijken, P ;
Joore, J ;
Peppelenbosch, MP .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (47) :49206-49213
[10]   Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae [J].
Ficarro, SB ;
McCleland, ML ;
Stukenberg, PT ;
Burke, DJ ;
Ross, MM ;
Shabanowitz, J ;
Hunt, DF ;
White, FM .
NATURE BIOTECHNOLOGY, 2002, 20 (03) :301-305