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Biochem Biophys Res Commun. 2007 Nov 16;363(2):375-80. Epub 2007 Sep 10.

Novel subsets of the Arabidopsis plasmalemma phosphoproteome identify phosphorylation sites in secondary active transporters.

Author information

1
Laboratoire de Protéomique Fonctionnelle, UR1199, INRA, F-34060 Montpellier, France. hem@supagro.inra.fr

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.

PMID:
17869214
DOI:
10.1016/j.bbrc.2007.08.177
[Indexed for MEDLINE]

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