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A proteomic and phosphoproteomic analysis of Oryza sativa plasma membrane and vacuolar membrane

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JournalPlant Journal
DatePublished - Oct 2008
Issue number1
Volume56
Number of pages10
Pages (from-to)146-156
Original languageEnglish

Abstract

Proteomic and phosphoproteomic analyses of rice shoot and root tonoplast-enriched and plasma membrane-enriched membrane fractions were carried out to look at tissue-specific expression, and to identify putative regulatory sites of membrane transport proteins. Around 90 unique membrane proteins were identified, which included primary and secondary transporters, ion channels and aquaporins. Primary H+ pumps from the AHA family showed little isoform specificity in their tissue expression pattern, whereas specific isoforms of the Ca2+ pump ECA/ACA family were expressed in root and shoot tissues. Several ABC transporters were detected, particularly from the MDR and PDR subfamilies, which often showed expression in either roots or shoots. Ammonium transporters were expressed in root, but not shoot, tissue. Large numbers of sugar transporters were expressed, particularly in green tissue. The occurrence of phosphorylation sites in rice transporters such as AMT1;1 and PIP2;6 agrees with those previously described in other species, pointing to conserved regulatory mechanisms. New phosphosites were found in many transporters, including H+ pumps and H+:cation antiporters, often at residues that are well conserved across gene families. Comparison of root and shoot tissue showed that phosphorylation of AMT1;1 and several further transporters may be tissue dependent.

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© 2008 The Authors. This is an author produced version of a paper published in Plant Journal. Uploaded in accordance with the publisher's self archiving policy.

    Research areas

  • proteomics, phosphoproteomics, membrane transport, Oryza sativa, rice, ARABIDOPSIS-THALIANA, ABC TRANSPORTER, H+-ATPASE, K+ UPTAKE, PLANT, RICE, PROTEINS, IDENTIFICATION, EXPRESSION, REVEALS

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