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Plant Cell Advance Online Publication
Published on May 4, 2007; 10.1105/tpc.105.035626

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Received June 29, 2006
Returned for revision April 3, 2007
Accepted April 17, 2007

Arabidopsis Protein Kinase PKS5 Inhibits the Plasma Membrane H+-ATPase by Preventing Interaction with 14-3-3 Protein

Anja T. Fuglsang 1, Yan Guo 2, Tracey A. Cuin 3, Quansheng Qiu 2, Chunpeng Song 2, Kim A. Kristiansen 1, Katrine Bych 1, Alexander Schulz 1, Sergey Shabala 3, Karen S. Schumaker 2, Michael G. Palmgren 1*, and Jian-Kang Zhu 2

1 Department of Plant Biology, University of Copenhagen, DK-1871 Frederiksberg C, Denmark
2 Department of Plant Sciences, University of Arizona, Tucson, Arizona 85721
3 School of Agricultural Sciences, University of Tasmania, Hobart TAS 7001, Australia

* To whom correspondence should be addressed. E-mail: palmgren{at}life.ku.dk.

Regulation of the trans-plasma membrane pH gradient is an important part of plant responses to several hormonal and environmental cues, including auxin, blue light, and fungal elicitors. However, little is known about the signaling components that mediate this regulation. Here, we report that an Arabidopsis thaliana Ser/Thr protein kinase, PKS5, is a negative regulator of the plasma membrane proton pump (PM H+-ATPase). Loss-of-function pks5 mutant plants are more tolerant of high external pH due to extrusion of protons to the extracellular space. PKS5 phosphorylates the PM H+-ATPase AHA2 at a novel site, Ser-931, in the C-terminal regulatory domain. Phosphorylation at this site inhibits interaction between the PM H+-ATPase and an activating 14-3-3 protein in a yeast expression system. We show that PKS5 interacts with the calcium binding protein SCaBP1 and that high external pH can trigger an increase in the concentration of cytosolic-free calcium. These results suggest that PKS5 is part of a calcium-signaling pathway mediating PM H+-ATPase regulation.






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