3 years ago

N-terminal S-acylation facilitates tonoplast targeting of the calcium sensor CBL6

Chunxia Zhang, Oliver Batistič, Linda Beckmann, Jörg Kudla
Protein S-acylation is important for many biological processes. It confers proteins with the ability to attach to the plasma membrane and the membranes confining the ER and Golgi compartments. Yet, the contribution of S-acylation to regulating and targeting lysosomal/vacuolar proteins remain largely enigmatic. Here, we report that vacuolar targeting of the calcium sensor calcineurin B-like protein 6 (CBL6) from Arabidopsis thaliana is brought about by S-acylation of N-terminal Cysteine residues. Our results suggest distinctions in mechanisms and efficiency of targeting between CBL6 and the previously characterized vacuolar-targeted CBL2 protein. Moreover, we define which CBL-interacting protein kinases (CIPKs) could interact with CBL6 and observe a remarkable temperature dependence of CBL6/CIPK complex formation. Collectively, these findings indicate a common S-acylation-dependent vacuolar membrane targeting pathway for proteins. This article is protected by copyright. All rights reserved.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/1873-3468.12880

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