N‐terminal S‐acylation facilitates tonoplast targeting of the calcium sensor CBL6
N‐terminal S‐acylation facilitates tonoplast targeting of the calcium sensor CBL6
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DOI：
10.1002/1873-3468.12880
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发表时间：
2017-11
期刊：
影响因子：
3.5
通讯作者：
Chunxia Zhang;Linda Beckmann;J. Kudla;Oliver Batistič
中科院分区：
文献类型：
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作者：
Chunxia Zhang;Linda Beckmann;J. Kudla;Oliver Batistič
蛋白质S-酰化对于许多生物过程是重要的。它赋予蛋白质附着于质膜和限制ER和高尔基体区室的膜的能力。然而，S-酰化对调节和靶向溶酶体/液泡蛋白的贡献在很大程度上仍然是谜。在这里，我们报告了拟南芥钙传感器钙调神经磷酸酶B样蛋白6（CBL 6）的液泡靶向是由N-末端半胱氨酸残基的S-酰化引起的。我们的研究结果表明CBL 6和先前表征的空泡靶向CBL 2蛋白之间的靶向机制和效率存在差异。此外，我们定义了哪些CBL相互作用蛋白激酶（CIPKs）可以与CBL 6相互作用，并观察到CBL 6/CIPK复合物形成的显着温度依赖性。总的来说，这些发现表明蛋白质存在一种常见的S-酰化依赖性液泡膜靶向途径。
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 remains 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‐acyla tion‐dependent vacuolar membrane targeting pathway for proteins.