First published online May 4, 2007; 10.1105/tpc.105.035626
The Plant Cell 19:1617-1634 (2007)
© 2007 American Society of Plant Biologists
Arabidopsis Protein Kinase PKS5 Inhibits the Plasma Membrane H+-ATPase by Preventing Interaction with 14-3-3 Protein
Anja T. Fuglsanga,1,
Yan Guob,1,2,
Tracey A. Cuinc,
Quansheng Qiub,
Chunpeng Songb,
Kim A. Kristiansena,
Katrine Bycha,
Alexander Schulza,
Sergey Shabalac,
Karen S. Schumakerb,
Michael G. Palmgrena,3 and
Jian-Kang Zhub,4
a Department of Plant Biology, University of Copenhagen, DK-1871 Frederiksberg C, Denmark
b Department of Plant Sciences, University of Arizona, Tucson, Arizona 85721
c School of Agricultural Sciences, University of Tasmania, Hobart TAS 7001, Australia
3 To whom correspondence should be addressed. E-mail palmgren{at}life.ku.dk; fax 45-3528 3365.
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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