Sorting and turnover of tonoplast proteins: the Arabidopsis potassium channel TPK1 as a model (Comunicazione a convegno)

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  • Sorting and turnover of tonoplast proteins: the Arabidopsis potassium channel TPK1 as a model (Comunicazione a convegno) (literal)
Anno
  • 2010-01-01T00:00:00+01:00 (literal)
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  • Maîtrejean M., Wudick M.M., Voelker C., Pedrazzini E., Czempinski K., Vitale A. (2010)
    Sorting and turnover of tonoplast proteins: the Arabidopsis potassium channel TPK1 as a model
    in IWPMB 2010, XV International Workshop on Plant Membrane Biology, Adelaide, Australia
    (literal)
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  • Maîtrejean M., Wudick M.M., Voelker C., Pedrazzini E., Czempinski K., Vitale A. (literal)
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  • Comunicazione orale su invito nella Session 9 - Membrane Structure, Development, Lipid Signalling and Lipid-transporter interactions, scelta dagli organizzatori fra i riassunti dei poster. (literal)
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  • 19-24/09/2010 (literal)
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  • We are using the potassium channel AtTPK1 of the Arabidopsis tonoplast as a model to study the synthesis, sorting and turnover of tonoplast proteins. Starting from a TPK1-GFP fusion, domains were substituted by the corresponding ones of the plasma membrane homologue AtTPK4. Transient expression in Arabidopsis protoplasts indicated that the cytosolic C-terminus of AtTPK1 is necessary and sufficient for tonoplast sorting of an AtTPK1/TPK4 fusion. TPK1-GFP formed dimers both in transgenic Arabidopsis and in transiently transformed protoplasts, whereas a number of TPK1/TPK4 fusions that remained located in the endoplasmic reticulum (ER) were unable to assemble correctly and interacted extensively with the ER chaperone BiP. This indicated that chimeric fusions remained in the ER because of conformational defects leading to retention by ER quality control rather than because they lack ER export signals. Pulse-chase experiments of protoplasts isolated from transgenic plants indicated that TPK1-GFP has a half life time of at least 24 hours and that its slow turnover involves internalization into the vacuole, leading to the vacuolar accumulation of soluble, released GFP that was originally fused to the C-terminus. This finding indicates a possible mechanism of turnover for tonoplast proteins. Supported by the EU Marie Curie RTN ‘VaTEP’ (MRTN-CT-2006–035833). (literal)
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  • MM, EP, AV: IBBA-CNR; MMW, CV, KC: University of Potsdam (Germany) (literal)
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  • Sorting and turnover of tonoplast proteins: the Arabidopsis potassium channel TPK1 as a model (literal)
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