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FEBS Lett. 2006 Feb 6;580(3):932-9. Epub 2006 Jan 18.

A WNK kinase binds and phosphorylates V-ATPase subunit C.

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  • 1Universität Tübingen, ZMBP-Plant Physiology, Auf der Morgenstelle 1, 72076 Tübingen, Germany.


WNK (with no lysine (K)) protein kinases are found in many eukaryotes and share a unique active site. Here, we report that a member of the Arabidopsis WNK family (AtWNK8) interacts with subunit C of the vacuolar H+-ATPase (V-ATPase) via a short C-terminal domain. AtWNK8 is shown to autophosphorylate intermolecularly and to phosphorylate Arabidopsis subunit C (AtVHA-C) at multiple sites as determined by MALDI-TOF MS analysis. Furthermore, we show that AtVHA-C and other V-ATPase subunits are phosphorylated when V1-complexes are used as substrates for AtWNK8. Taken together, our results provide evidence that V-ATPases are potential targets of WNK kinases and their associated signaling pathways.

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