| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
|
|
|
|||||||
|
|||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Submitted on April 12, 2007
Max-Planck Institut für molekulare Pflanzenphysiologie, Golm 14476
Corresponding Author: wschulze{at}mpimp-golm.mpg-de
Sucrose is the main product of photosynthesis and the most common transport form of carbon in plants. In addition, sucrose is a compound that serves as a signal affecting metabolic flux and development. Here we provide first results of externally induced phosphorylation changes of plasma membrane proteins in Arabidopsis. In an unbiased approach, seedlings were grown in liquid media with sucrose, then depleted of carbon before sucrose was resupplied. Plasma membranes were purified, phosphopeptides enriched, and subsequently analyzed quantitatively by mass spectrometry. In total, 67 phosphopeptides were identified, most of which were quantified over five time points of sucrose resupply. Among the identified phosphorylation sites, the well-described phosphorylation site at the C-terminus of plasma membrane H+-ATPases shows a relative increase in phosphorylation level in response to sucrose. This corresponded to a significant increase of proton pumping activity of plasma membrane vesicles from sucrose supplied seedlings. A new phosphorylation site was identified in the plasma membrane H+-ATPase AHA1 and/or AHA2. This phosphorylation site was shown to be crucial for ATPase activity and overrode regulation via the well-known C-terminal phosphorylation site. Novel phosphorylation sites were identified for both receptor kinases and cytosolic kinases which show rapid increases in relative intensities after short times of sucrose treatment. Seven response classes were identified including non-responsive, rapid-increase (within 3 min), slow-increase, and rapid-decrease. Relative quantification of phosphorylation changes by phosphoproteomics provides a means for identification of fast responses to external stimuli in plants as a basis for further functional characterization.
Revised on June 1, 2007
Accepted on June 22, 2007
Temporal analysis of sucrose-induced phosphorylation changes in plasma membrane proteins of Arabidopsis
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  W. Tang, T.-W. Kim, J. A. Oses-Prieto, Y. Sun, Z. Deng, S. Zhu, R. Wang, A. L. Burlingame, and Z.-Y. Wang BSKs Mediate Signal Transduction from the Receptor Kinase BRI1 in Arabidopsis Science, July 25, 2008; 321(5888): 557 - 560. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Prak, S. Hem, J. Boudet, G. Viennois, N. Sommerer, M. Rossignol, C. Maurel, and V. Santoni Multiple Phosphorylations in the C-terminal Tail of Plant Plasma Membrane Aquaporins: Role in Subcellular Trafficking of AtPIP2;1 in Response to Salt Stress Mol. Cell. Proteomics, June 1, 2008; 7(6): 1019 - 1030. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. L. Heazlewood, P. Durek, J. Hummel, J. Selbig, W. Weckwerth, D. Walther, and W. X. Schulze PhosPhAt: a database of phosphorylation sites in Arabidopsis thaliana and a plant-specific phosphorylation site predictor Nucleic Acids Res., January 11, 2008; 36(suppl_1): D1015 - D1021. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. J. Thelen and S. C. Peck Quantitative Proteomics in Plants: Choices in Abundance PLANT CELL, November 1, 2007; 19(11): 3339 - 3346. [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| All ASBMB Journals | Journal of Biological Chemistry |
| Journal of Lipid Research | ASBMB Today |
