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Dual Fatty Acyl Modification Determines the Localization and Plasma Membrane Targeting of CBL/CIPK Ca²⁺ Signaling Complexes in Arabidopsis^[W]

Oliver Batisti^a, Nadav Sorek^b, Stefanie Schültke^a, Shaul Yalovsky^b and Jörg Kudla^a,1

^a Institut für Botanik, Universität Münster, 48149 Münster, Germany
^b Department of Plant Sciences, Tel Aviv University, Ramat Aviv, Tel Aviv 69978, Israel

¹ Address correspondence to jkudla{at}uni-muenster.de.

Arabidopsis thaliana calcineurin B–like proteins (CBLs) interact specifically with a group of CBL-interacting protein kinases (CIPKs). CBL/CIPK complexes phosphorylate target proteins at the plasma membrane. Here, we report that dual lipid modification is required for CBL1 function and for localization of this calcium sensor at the plasma membrane. First, myristoylation targets CBL1 to the endoplasmic reticulum. Second, S-acylation is crucial for endoplasmic reticulum-to-plasma membrane trafficking via a novel cellular targeting pathway that is insensitive to brefeldin A. We found that a 12–amino acid peptide of CBL1 is sufficient to mediate dual lipid modification and to confer plasma membrane targeting. Moreover, the lipid modification status of the calcium sensor moiety determines the cellular localization of preassembled CBL/CIPK complexes. Our findings demonstrate the importance of S-acylation for regulating the spatial accuracy of Ca²⁺-decoding proteins and suggest a novel mechanism that enables the functional specificity of calcium sensor/kinase complexes.