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Plant Cell, Vol. 11, 2393-2406, December 1999, Copyright © 1999, American Society of Plant Physiologists

Novel Protein Kinases Associated with Calcineurin B–like Calcium Sensors in Arabidopsis

Jinrui Shia, Kyung-Nam Kima, Olga Ritzb, Veronica Albrechtb, Rajeev Guptaa, Klaus Harterc, Sheng Luana, and Jörg Kudlab
a Department of Plant and Microbial Biology, University of California, Berkeley, California 94720
b Universität Ulm, Abteilung Allgemeine Botanik, D-89069 Ulm, Germany
c Institut für Biology II/Botanik, Universität Freiburg, Schänzlestrasse 1, D-79104, Freiburg, Germany

Correspondence to: Sheng Luan, sluan{at}nature.berkeley.edu (E-mail), 510-642-4995 (fax)

Members of the Arabidopsis calcineurin B–like Ca2+ binding protein (AtCBL) family are differentially regulated by stress conditions. One AtCBL plays a role in salt stress; another is implicated in response to other stress signals, including drought, cold, and wounding. In this study, we identified a group of novel protein kinases specifically associated with AtCBL-type Ca2+ sensors. In addition to a typical protein kinase domain, they all contain a unique C-terminal region that is both required and sufficient for interaction with the AtCBL-type but not calmodulin-type Ca2+ binding proteins from plants. Interactions between the kinases and AtCBLs require micromolar concentrations of Ca2+, suggesting that increases in cellular Ca2+ concentrations may trigger the formation of AtCBL–kinase complexes in vivo. Unlike most serine/threonine kinases, the AtCBL-interacting kinase efficiently uses Mn2+ to Mg2+ as a cofactor and may function as a Mn2+ binding protein in the cell. These findings link a new type of Ca2+ sensors to a group of novel protein kinases, providing the molecular basis for a unique Ca2+ signaling machinery in plant cells.




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