Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2053069 | FEBS Letters | 2006 | 8 Pages |
Abstract
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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Authors
Anne Hong-Hermesdorf, Angela Brüx, Ardina Grüber, Gerhard Grüber, Karin Schumacher,