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Novel subsets of the Arabidopsis plasmalemma phosphoproteome identify phosphorylation sites in secondary active transporters
- Source :
-
Biochemical & Biophysical Research Communications . Nov2007, Vol. 363 Issue 2, p375-380. 6p. - Publication Year :
- 2007
-
Abstract
- Abstract: The generation of novel subsets of phosphorylation sites is needed to complement the present Arabidopsis plasma membrane phosphoprotein repertoire, where several families of proteins are under-represented. In this work, different combinations of chromatographic steps were first compared for capacity to resolve model phosphopeptides before characterisation from PSD fragments in MALDI MS/MS. Nearly half of the phosphorylation sites detected in the Arabidopsis plasmalemma using the optimised procedure were novel, and two-thirds of protein accessions identified secondary active transporters. These included phosphate/H+ symporters, ammonium and nitrate transporters, different alkali cation exchangers, a urea/H+ symporter, a glucose transporter, a purine permease, and peptide transporters. There has been previous functional evidence for phosphorylation of only a minority of these, the regulation of others having been essentially investigated at the transcriptional level. The demonstration of active phosphorylation sites in such a diverse set of secondary transporter families suggests that this regulation level plays a major role in the response of plants to nutrient availability. [Copyright &y& Elsevier]
- Subjects :
- *BIOLOGY
*BIOPHYSICS
*BIOCHEMISTRY
*LIFE sciences
Subjects
Details
- Language :
- English
- ISSN :
- 0006291X
- Volume :
- 363
- Issue :
- 2
- Database :
- Academic Search Index
- Journal :
- Biochemical & Biophysical Research Communications
- Publication Type :
- Academic Journal
- Accession number :
- 26822307
- Full Text :
- https://doi.org/10.1016/j.bbrc.2007.08.177