Proteomic analysis of phosphorylated proteins

Current Opinion in Plant Biology

Volumn 9, Issue 5, 2006, Pages 538-543

  Rossignol, Michel ^a  

^a CEMAGREF   (France)

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOTRANSFERASE; VEGETABLE PROTEIN;

BIOLOGY; METABOLISM; METHODOLOGY; PHOSPHORYLATION; PLANT; PROTEOMICS; REVIEW;

COMPUTATIONAL BIOLOGY; PHOSPHORYLATION; PHOSPHOTRANSFERASES; PLANT PROTEINS; PLANTS; PROTEOMICS;

EID: 33747888494     PISSN: 13695266     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pbi.2006.07.004     Document Type: Review

References (34)

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11. •] upstream of MS analysis.
12. 4 neutral loss peak observed in classical MS/MS is shown to constitute a useful strategy to facilitate or confirm the identification of phosphorylation sites.
13. Larsen M.R., Thingholm T.E., Jensen O.N., Roepstorff P., and Jorgensen T.J.D. Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol Cell Proteomics 4 (2005) 873-886
14. 2 chromatography procedure that was recently reported as being more efficient than classical IMAC [13]. The authors describe very encouraging results for complex samples of spinach stromal proteins, including the demonstration of several previously undetected phosphorylation sites.
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23. Hong-Hermesdorf A., Brüx A., Grüber A., Grüber G., and Schumacher K. A WNK kinase binds and phosphorylates V-ATPase subunit C. FEBS Lett 580 (2006) 932-939. Using classical molecular and proteomic approaches, the authors demonstrate that AtWNK8 is the second member of the Arabidopsis WNK protein kinase family known to be able to phosphorylate a protein. They identify the vacuolar ATPase as a potential target.
24. Wang X., Goshe M.B., Soderblom E.J., Phinney B.S., Kuchar J.A., Li J., Asami T., Yoshida S., Huber S.C., and Clouse S.D. Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase. Plant Cell 17 (2005) 1685-1703. This very interesting paper describes a simple but powerful combination of biochemical approaches to map the phosphorylation sites in BRI1 and to characterize sites that are potentially involved in early events of brassinosteroid signaling. In conjunction with site-directed mutagenesis experiments, two out the eleven phosphorylation sites detected were proposed to be required for the function of this receptor-like kinase.
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31. Irar S., Oliveira E., Pagès M., and Goday A. Towards the identification of late-embryogenic-abundant phosphoproteome in Arabidopsis by 2-DE and MS. Proteomics 6 (2006) S175-S185. This work constitutes the first example in plants of the use of the recently available commercial tools for phosphoproteomics. The authors describe consistent and promising results obtained using phosphoprotein enrichment by affinity chromatography kits and phosphoprotein-specific detection on gels. However, these results were not validated by the characterization of phosphorylation sites.
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33. Nühse T.S., Stensballe A., Jensen O.N., and Peck S.C. Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database. Plant Cell 16 (2004) 2394-2405. This very innovative paper delivers the first conclusions about the features of plant phosphorylation sites, as derived by mining large-scale datasets produced by modern phosphoproteomics approaches.
34. Rudrabhatla P., Reddy M.M., and Rajasekharan R. Genome-wide analysis and experimentation of plant serine/threonine/tyrosine-specific protein kinases. Plant Mol Biol 60 (2006) 293-319. The authors begin with a bioinformatic analysis of the set of proteins showing a tyrosine-kinase domain in Arabidopsis. They then use a typical example from among these proteins to show that such kinases are also able to autophosphorylate their own serine and threonine residues, although this activity is not as great as that at tyrosine residues.