Wingenter, Karina and Trentmann, Oliver and Winschuh, Irina and Hoermiller, Imke I. and Heyer, Arnd G. and Reinders, Joerg and Schulz, Alexander and Geiger, Dietmar and Hedrich, Rainer and Neuhaus, H. Ekkehard (2011) A member of the mitogen-activated protein 3-kinase family is involved in the regulation of plant vacuolar glucose uptake. PLANT JOURNAL, 68 (5). pp. 890-900. ISSN 0960-7412, 1365-313X
Full text not available from this repository. (Request a copy)Abstract
Vacuolar solute accumulation is an important process during plant development, growth and stress responses. Although several vacuolar carriers have been identified recently, knowledge regarding the regulation of transport is still limited. Solute accumulation may be controlled by various factors, such as alterations in carrier abundance or activity. Phosphorylation via kinases is a well-known principle for activation or deactivation of proteins. Several phosphorylated proteins have been identified in the tonoplast proteome; however, kinases that catalyse the phosphorylation of tonoplast proteins are currently unknown. The tonoplast monosaccaride transporter from Arabidopsis (AtTMT1) and its homologue from barley have multiple phosphorylation sites in their extremely large loops. Here we demonstrate that the loop of AtTMT1 interacts with a mitogen-activated triple kinase-like protein kinase (VIK), that an aspartate-rich loop domain is required for effective interaction, and that the presence of VIK stimulates glucose import into isolated vacuoles. Furthermore, the phenotype of VIK loss-of-function plants strikingly resembles that of plants lacking AtTMT1/2. These data suggest that VIK-mediated phosphorylation of the AtTMT1 loop enhances carrier activity and consequently vacuolar sugar accumulation. As many phosphorylated proteins have been identified in the tonoplast, differential phosphorylation may be a general mechanism regulating vacuolar solute import.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | MONOSACCHARIDE TRANSPORTERS; PHOSPHORYLATION SITES; ARABIDOPSIS-THALIANA; SUGAR-TRANSPORT; IDENTIFICATION; METABOLISM; TONOPLAST; GROWTH; ACCUMULATION; EXPRESSION; glucose; vacuole; MAP 3-kinase; major facilitator superfamily; transport; Arabidopsis |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Institut für Funktionelle Genomik > Lehrstuhl für Funktionelle Genomik (Prof. Oefner) |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 26 May 2020 06:58 |
| Last Modified: | 26 May 2020 06:58 |
| URI: | https://pred.uni-regensburg.de/id/eprint/19726 |
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