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Identification of a Calmodulin-Regulated Ca2+-ATPase in the Endoplasmic Reticulum1

Bimei Hong, Audrey Ichida, Yuwen Wang, J. Scott Gens, Barbara G. Pickard, and Jeffrey F. Harper*

Department of Cell Biology, The Scripps Research Institute, BCC283, 10550 North Torrey Pines Road, La Jolla, California 92037 (B.H., Y.W., J.F.H.); and Department of Biology, Washington University, St. Louis, Missouri 63130-4899 (A.I., J.S.G., B.G.P.)

A unique subfamily of calmodulin-dependent Ca2+-ATPases was recently identified in plants. In contrast to the most closely related pumps in animals, plasma membrane-type Ca2+-ATPases, members of this new subfamily are distinguished by a calmodulin-regulated autoinhibitor located at the N-terminal instead of a C-terminal end. In addition, at least some isoforms appear to reside in non-plasma membrane locations. To begin delineating their functions, we investigated the subcellular localization of isoform ACA2p (Arabidopsis Ca2+-ATPase, isoform 2 protein) in Arabidopsis. Here we provide evidence that ACA2p resides in the endoplasmic reticulum (ER). In buoyant density sucrose gradients performed with and without Mg2+, ACA2p cofractionated with an ER membrane marker and a typical "ER-type" Ca2+-ATPase, ACA3p/ECA1p. To visualize its subcellular localization, ACA2p was tagged with a green fluorescence protein at its C terminus (ACA2-GFPp) and expressed in transgenic Arabidopsis. We collected fluorescence images from live root cells using confocal and computational optical-sectioning microscopy. ACA2-GFPp appeared as a fluorescent reticulum, consistent with an ER location. In addition, we observed strong fluorescence around the nuclei of mature epidermal cells, which is consistent with the hypothesis that ACA2p may also function in the nuclear envelope. An ER location makes ACA2p distinct from all other calmodulin-regulated pumps identified in plants or animals.

1   This research was supported by a U.S. Department of Energy grant (no. DE-FG03-94ER20152) to J.F.H. and a joint grant (no. IBN-9416038) from the National Aeronautics and Space Administration and the National Science Foundation for the Plant Sensory Systems Collaborative Research Network. Support for computational microscopy was provided by a National Institutes of Health grant (no. RR01380) to the Institute for Biomedical Computing at Washington University and to J.S.G. through a Monsanto predoctoral fellowship in plant biology.
*   Corresponding author; e-mail Harper{at}Scripps.edu; fax 1- 619-784-9840.

Plant Physiol. (1999) 119: 1165-1176
Copyright Clearance Center:   0032-0889/99/119//12
© 1999 American Society of Plant Physiologists




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