Identification of tonoplast membrane proteins involved in cellular response to environmental stress by quantitative/comparative- and phospho-proteomics
Final Report Abstract
During the recent funding period we were able to identify protein interactions between all members of the MAPK3 subgroup C1. Furthermore all VIK proteins seem to interact with a so far not described plasmamembrane located receptor like kinase. These data indicate a protein phosphorylation based signaling pathway/network from the plasmamembrane towards the vacuole regulating the activity of the tonoplast sugar transporters (TST). The “Forschergruppe” 1061 enabled the development of purification protocols suitable for comparative proteome analyses of tonoplast membrane proteins. By these proteome analyses will help to further understand the significance of this sizeable cell compartment in the plants adaptation to environmental changes and how vacuolar proteins are regulated and are embedded into cellular signaling pathways. We have established several fruitful cooperation that will outlast the FOR 1061 and hopeful lead to further funding.
Publications
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(2013) Current progress in tonoplast proteomics reveals insights into the function of the large central vacuole. Review, Front. Plant Sci. 4:34
Trentmann, O. and Haferkamp I.
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(2014) Overexpression of a proton-coupled vacuolar glucose exporter impairs freezing tolerance and seed germination. New Phytol. 202: 188-197
Klemens, P.A.W., Patzke, K., Trentmann, O., Poschet, G., Büttner, M., Schulz, A., Marten, I., Hedrich, R., Neuhaus, H.E.
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(2014) Regulation of transport processes across the tonoplast. Front. Plant Sci. 5:460
Neuhaus, H.E., and Trentmann, O.
