S-acylation-dependent association of the calcium sensor CBL2 with the vacuolar membrane is essential for proper abscisic acid responses

被引:85
作者
Batistic, Oliver [1 ]
Rehers, Marion [1 ]
Akerman, Amir [2 ]
Schluecking, Kathrin [1 ]
Steinhorst, Leonie [1 ]
Yalovsky, Shaul [2 ]
Kudla, Joerg [1 ]
机构
[1] Univ Munster, Inst Biol & Biotechnol Pflanzen, D-48149 Munster, Germany
[2] Tel Aviv Univ, Dept Mol Biol & Ecol Plants, IL-69978 Tel Aviv, Israel
基金
以色列科学基金会;
关键词
S-acylation; vacuolar membrane; ABA; CBL; calcium; B-LIKE PROTEINS; PALMITOYLATION; ARABIDOPSIS; LOCALIZATION; KINASE; SIGNALS; ACYLTRANSFERASES; SENSITIVITY; DETERMINES; TISSUE;
D O I
10.1038/cr.2012.71
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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.
引用
收藏
页码:1155 / 1168
页数:14
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