Volume 22, No 7, Jul 2012
ISSN: 1001-0602
EISSN: 1748-7838 2018
impact factor 17.848*
(Clarivate Analytics, 2019)
Volume 22 Issue 7, July 2012: 1155-1168
ORIGINAL ARTICLES
S-acylation-dependent association of the calcium sensor CBL2 with the vacuolar membrane is essential for proper abscisic acid responses
Oliver Batistič1, Marion Rehers1, Amir Akerman2, Kathrin Schlücking2, Leonie Steinhorst1, Shaul Yalovsky2 and Jörg Kudla1
1Institut f黵 Biologie und Biotechnologie der Pflanzen, Universit鋞 Münster, Schlossplatz 4, M黱ster 48149, Germany
2Department of Molecular Biology and Ecology of Plants, Tel Aviv University, Ramat Aviv, Tel Aviv 69978, Israel
Correspondence: J鰎g Kudla,(jkudla@uni-muenster.de)
Calcineurin B-like (CBL) proteins contribute to decoding calcium signals by interacting with CBL-interacting protein kinases (CIPKs). Currently, there is still very little information about the function and specific targeting mechanisms of CBL proteins that are localized at the vacuolar membrane. In this study, we focus on CBL2, an abundant vacuolar membrane-localized calcium sensor of unknown function from Arabidopsis thaliana. We show that vacuolar targeting of CBL2 is specifically brought about by S-acylation of three cysteine residues in its N-terminus and that CBL2 S-acylation and targeting occur by a Brefeldin A-insensitive pathway. Loss of CBL2 function renders plants hypersensitive to the phytohormone abscisic acid (ABA) during seed germination and only fully S-acylated and properly vacuolar-targeted CBL2 proteins can complement this mutant phenotype. These findings define an S-acylation-dependent vacuolar membrane targeting pathway for proteins and uncover a crucial role of vacuolar calcium sensors in ABA responses.
Cell Research (2012) 22:1155-1168. doi:10.1038/cr.2012.71; published online 1 May 2012
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