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First published online July 10, 2003; 10.1104/pp.103.020008

Plant Physiology 132:1840-1848 (2003)
© 2003 American Society of Plant Biologists

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CELL BIOLOGY AND SIGNAL TRANSDUCTION

Subcellular Targeting of Nine Calcium-Dependent Protein Kinase Isoforms from Arabidopsis1

Christian Dammann2, Audrey Ichida2, Bimei Hong, Shawn M. Romanowsky, Estelle M. Hrabak, Alice C. Harmon, Barbara G. Pickard and Jeffrey F. Harper*

Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037 (C.D., B.H., S.M.R., J.F.H.); Biology Department, Washington University, St. Louis, Missouri 63130–4899 (A.I., B.G.P.); Department of Plant Biology, University of New Hampshire, 46 College Road, Durham, New Hampshire 03824 (E.M.H.); and Botany Department, University of Florida, Gainesville, Florida 32611–8526 (A.C.H.)

Calcium-dependent protein kinases (CDPKs) are specific to plants and some protists. Their activation by calcium makes them important switches for the transduction of intracellular calcium signals. Here, we identify the subcellular targeting potentials for nine CDPK isoforms from Arabidopsis, as determined by expression of green fluorescent protein (GFP) fusions in transgenic plants. Subcellular locations were determined by fluorescence microscopy in cells near the root tip. Isoforms AtCPK3-GFP and AtCPK4-GFP showed a nuclear and cytosolic distribution similar to that of free GFP. Membrane fractionation experiments confirmed that these isoforms were primarily soluble. A membrane association was observed for AtCPKs 1, 7, 8, 9, 16, 21, and 28, based on imaging and membrane fractionation experiments. This correlates with the presence of potential N-terminal acylation sites, consistent with acylation as an important factor in membrane association. All but one of the membrane-associated isoforms targeted exclusively to the plasma membrane. The exception was AtCPK1-GFP, which targeted to peroxisomes, as determined by covisualization with a peroxisome marker. Peroxisome targeting of AtCPK1-GFP was disrupted by a deletion of two potential N-terminal acylation sites. The observation of a peroxisome-located CDPK suggests a mechanism for calcium regulation of peroxisomal functions involved in oxidative stress and lipid metabolism.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.103.020008.

1 This work was supported in part by the Department of Energy (grant no. DE–FG03–94ER20152 to J.F.H.), by the National Science Foundation (grant nos. MCB011476 and IBN-9416038 to J.F.H.), by the Human Frontiers Science Program (grant no. RG0268to J.F.H.), by Syngenta (to J.F.H.), by the National Aeronautics and Space Administration/National Science Foundation Joint Program in Plant Biology (grant no. NAGW 3046 to B.G.P.), and by the National Science Foundation (grant no. MCB 9973770 to A.C.H.).

2 These authors contributed equally to the paper.

* Corresponding author; e-mail Harper{at}Scripps.edu; fax 858–784–9840.

Received January 3, 2003; returned for revision February 5, 2003; accepted April 21, 2003.


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