Interplay of vacuolar transporters for coupling primary and secondary active transport

Michèle Siek; Berenice Marg; Chris M. Ehring; Derya Kirasi; Michael Liebthal; Thorsten Seidel; Michèle Siek; Berenice Marg; Chris M. Ehring; Derya Kirasi; Michael Liebthal; Thorsten Seidel

doi:10.3934/biophy.2016.4.479

AIMS Biophysics

2016, Volume 3, Issue 4: 479-500. doi: 10.3934/biophy.2016.4.479

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Research article Special Issues

Interplay of vacuolar transporters for coupling primary and secondary active transport

Dynamic Cell Imaging, Faculty of Biology, Bielefeld University, 33501 Bielefeld, Germany

Received: 30 August 2016 Accepted: 13 October 2016 Published: 24 October 2016

Secondary active transporters are driven by the proton motif force which is generated by primary active transporters such as the vacuolar proton pumps V-ATPase and V-PPase. The vacuole occupies up to 90 % of the mature cell and acidification of the vacuolar lumen is a challenging and energy-consuming task for the plant cell. Therefore, a direct coupling of primary and secondary active transporters is expected to enhance transport efficiency and to reduce energy consumption by transport processes across the tonoplast. This has been addressed by analyzing physical and functional interactions between the V-ATPase and a selection of vacuolar transporters including the primary active proton pump AVP1, the calcium ion/proton exchanger CAX1, the potassium ion/proton symporter KUP5, the sodium ion/proton exchanger NHX1, and the anion/proton exchanger CLC-c. Physical interaction was demonstrated in vivo for the V-ATPase and the secondary active transporters CAX1 and CLC-c, which are responsible for calcium- and anion-accumulation in the vacuole, respectively. Measurements of V-ATPase activity and vacuolar pH revealed a functional interaction of V-ATPase and CAX1, CLC-c that is likely caused by the observed physical interaction. The complex of the V-ATPase further interacts with the nitrate reductase 2, and as a result, nitrate assimilation is directly linked to the energization of vacuolar nitrate accumulation by secondary active anion/proton exchangers.
- vacuolar ATPase,
- proton motif force,
- secondary active transport,
- vacuole,
- protein-protein interaction
Citation: Michèle Siek, Berenice Marg, Chris M. Ehring, Derya Kirasi, Michael Liebthal, Thorsten Seidel. Interplay of vacuolar transporters for coupling primary and secondary active transport[J]. AIMS Biophysics, 2016, 3(4): 479-500. doi: 10.3934/biophy.2016.4.479

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Abstract

Secondary active transporters are driven by the proton motif force which is generated by primary active transporters such as the vacuolar proton pumps V-ATPase and V-PPase. The vacuole occupies up to 90 % of the mature cell and acidification of the vacuolar lumen is a challenging and energy-consuming task for the plant cell. Therefore, a direct coupling of primary and secondary active transporters is expected to enhance transport efficiency and to reduce energy consumption by transport processes across the tonoplast. This has been addressed by analyzing physical and functional interactions between the V-ATPase and a selection of vacuolar transporters including the primary active proton pump AVP1, the calcium ion/proton exchanger CAX1, the potassium ion/proton symporter KUP5, the sodium ion/proton exchanger NHX1, and the anion/proton exchanger CLC-c. Physical interaction was demonstrated in vivo for the V-ATPase and the secondary active transporters CAX1 and CLC-c, which are responsible for calcium- and anion-accumulation in the vacuole, respectively. Measurements of V-ATPase activity and vacuolar pH revealed a functional interaction of V-ATPase and CAX1, CLC-c that is likely caused by the observed physical interaction. The complex of the V-ATPase further interacts with the nitrate reductase 2, and as a result, nitrate assimilation is directly linked to the energization of vacuolar nitrate accumulation by secondary active anion/proton exchangers.

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