| Item type: | Article | ||||||||||||||||||||||||||||||||||||||||||||||
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| Journal or Publication Title: | The Plant journal | ||||||||||||||||||||||||||||||||||||||||||||||
| Publisher: | Wiley | ||||||||||||||||||||||||||||||||||||||||||||||
| Volume: | 68 | ||||||||||||||||||||||||||||||||||||||||||||||
| Number of Issue or Book Chapter: | 5 | ||||||||||||||||||||||||||||||||||||||||||||||
| Page Range: | pp. 890-900 | ||||||||||||||||||||||||||||||||||||||||||||||
| Date: | December 2011 | ||||||||||||||||||||||||||||||||||||||||||||||
| Institutions: | Medicine > Institut für Funktionelle Genomik > Lehrstuhl für Funktionelle Genomik (Prof. Oefner) | ||||||||||||||||||||||||||||||||||||||||||||||
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| Classification: |
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| Keywords: | glucose; vacuole; MAP 3-kinase; major facilitator superfamily; transport; Arabidopsis | ||||||||||||||||||||||||||||||||||||||||||||||
| Dewey Decimal Classification: | 500 Science > 500 Natural sciences & mathematics 500 Science > 570 Life sciences 600 Technology > 610 Medical sciences Medicine | ||||||||||||||||||||||||||||||||||||||||||||||
| Status: | Published | ||||||||||||||||||||||||||||||||||||||||||||||
| Refereed: | Yes, this version has been refereed | ||||||||||||||||||||||||||||||||||||||||||||||
| Created at the University of Regensburg: | Partially | ||||||||||||||||||||||||||||||||||||||||||||||
| Item ID: | 30619 |
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 ...
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.
Metadata last modified: 29 Sep 2021 07:40
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