A WNK kinase binds and phosphorylates V-ATPase subunit C
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...
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| Hauptverfasser: | , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
18 January 2006
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| In: |
FEBS letters
Year: 2006, Jahrgang: 580, Heft: 3, Pages: 932-939 |
| ISSN: | 1873-3468 |
| DOI: | 10.1016/j.febslet.2006.01.018 |
| Online-Zugang: | Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1016/j.febslet.2006.01.018 Verlag, kostenfrei, Volltext: http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2006.01.018/abstract 
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| Verfasserangaben: | Anne Hong-Hermesdorf, Angela Brüx, Ardina Grüber, Gerhard Grüber, Karin Schumacher |
| Zusammenfassung: | 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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| Beschreibung: | Gesehen am 09.05.2017 |
| Beschreibung: | Online Resource |
| ISSN: | 1873-3468 |
| DOI: | 10.1016/j.febslet.2006.01.018 |