Subcellular Targeting of Plant Sucrose Transporters Is Affected by Their Oligomeric State
Post-translational regulation of sucrose transporters represents one possibility to adapt transporter activity in a very short time frame. This can occur either via phosphorylation/dephosphorylation, oligomerization, protein−protein interactions, endocytosis/exocytosis, or degradation. It...
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MDPI AG
2020-01-01
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Online Access: | https://www.mdpi.com/2223-7747/9/2/158 |
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author | Varsha Garg Aleksandra Hackel Christina Kühn |
author_facet | Varsha Garg Aleksandra Hackel Christina Kühn |
author_sort | Varsha Garg |
collection | DOAJ |
description | Post-translational regulation of sucrose transporters represents one possibility to adapt transporter activity in a very short time frame. This can occur either via phosphorylation/dephosphorylation, oligomerization, protein−protein interactions, endocytosis/exocytosis, or degradation. It is also known that StSUT1 can change its compartmentalization at the plasma membrane and concentrate in membrane microdomains in response to changing redox conditions. A systematic screen for protein−protein-interactions of plant sucrose transporters revealed that the interactome of all three known sucrose transporters from the Solanaceous species <i>Solanum tuberosum</i> and <i>Solanum lycopersicum</i> represents a specific subset of interaction partners, suggesting different functions for the three different sucrose transporters. Here, we focus on factors that affect the subcellular distribution of the transporters. It was already known that sucrose transporters are able to form homo- as well as heterodimers. Here, we reveal the consequences of homo- and heterodimer formation and the fact that the responses of individual sucrose transporters will respond differently. Sucrose transporter SlSUT2 is mainly found in intracellular vesicles and several of its interaction partners are involved in vesicle traffic and subcellular targeting. The impact of interaction partners such as SNARE/VAMP proteins on the localization of SlSUT2 protein will be investigated, as well as the impact of inhibitors, excess of substrate, or divalent cations which are known to inhibit SUT1-mediated sucrose transport in yeast cells. Thereby we are able to identify factors regulating sucrose transporter activity via a change of their subcellular distribution. |
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language | English |
last_indexed | 2024-12-19T23:50:09Z |
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spelling | doaj.art-83562df13d5f4ad985eed4a4f0e9caf02022-12-21T20:01:10ZengMDPI AGPlants2223-77472020-01-019215810.3390/plants9020158plants9020158Subcellular Targeting of Plant Sucrose Transporters Is Affected by Their Oligomeric StateVarsha Garg0Aleksandra Hackel1Christina Kühn2Humboldt-Universität zu Berlin, Plant Physiology, Philippstr. 13, Building 12, 10115 Berlin, GermanyHumboldt-Universität zu Berlin, Plant Physiology, Philippstr. 13, Building 12, 10115 Berlin, GermanyHumboldt-Universität zu Berlin, Plant Physiology, Philippstr. 13, Building 12, 10115 Berlin, GermanyPost-translational regulation of sucrose transporters represents one possibility to adapt transporter activity in a very short time frame. This can occur either via phosphorylation/dephosphorylation, oligomerization, protein−protein interactions, endocytosis/exocytosis, or degradation. It is also known that StSUT1 can change its compartmentalization at the plasma membrane and concentrate in membrane microdomains in response to changing redox conditions. A systematic screen for protein−protein-interactions of plant sucrose transporters revealed that the interactome of all three known sucrose transporters from the Solanaceous species <i>Solanum tuberosum</i> and <i>Solanum lycopersicum</i> represents a specific subset of interaction partners, suggesting different functions for the three different sucrose transporters. Here, we focus on factors that affect the subcellular distribution of the transporters. It was already known that sucrose transporters are able to form homo- as well as heterodimers. Here, we reveal the consequences of homo- and heterodimer formation and the fact that the responses of individual sucrose transporters will respond differently. Sucrose transporter SlSUT2 is mainly found in intracellular vesicles and several of its interaction partners are involved in vesicle traffic and subcellular targeting. The impact of interaction partners such as SNARE/VAMP proteins on the localization of SlSUT2 protein will be investigated, as well as the impact of inhibitors, excess of substrate, or divalent cations which are known to inhibit SUT1-mediated sucrose transport in yeast cells. Thereby we are able to identify factors regulating sucrose transporter activity via a change of their subcellular distribution.https://www.mdpi.com/2223-7747/9/2/158subcellular targetingvesicle trafficmembrane microdomainssucrose transporterendocytosis |
spellingShingle | Varsha Garg Aleksandra Hackel Christina Kühn Subcellular Targeting of Plant Sucrose Transporters Is Affected by Their Oligomeric State Plants subcellular targeting vesicle traffic membrane microdomains sucrose transporter endocytosis |
title | Subcellular Targeting of Plant Sucrose Transporters Is Affected by Their Oligomeric State |
title_full | Subcellular Targeting of Plant Sucrose Transporters Is Affected by Their Oligomeric State |
title_fullStr | Subcellular Targeting of Plant Sucrose Transporters Is Affected by Their Oligomeric State |
title_full_unstemmed | Subcellular Targeting of Plant Sucrose Transporters Is Affected by Their Oligomeric State |
title_short | Subcellular Targeting of Plant Sucrose Transporters Is Affected by Their Oligomeric State |
title_sort | subcellular targeting of plant sucrose transporters is affected by their oligomeric state |
topic | subcellular targeting vesicle traffic membrane microdomains sucrose transporter endocytosis |
url | https://www.mdpi.com/2223-7747/9/2/158 |
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