Suppressor of K+ transport growth defect 1 (SKD1) interacts with RING-type ubiquitin ligase and sucrose non-fermenting 1-related protein kinase (SnRK1) in the halophyte ice plant.
Suppressor of K+ transport growth defect 1 (SKD1) interacts with RING-type ubiquitin ligase and sucrose non-fermenting 1-related protein kinase (SnRK1) in the halophyte ice plant.
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DOI：
10.1093/jxb/ert097
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发表时间：
2013-05
影响因子：
6.9
通讯作者：
Yen HE
中科院分区：
文献类型：
--
作者：
Chiang CP;Li CH;Jou Y;Chen YC;Lin YC;Yang FY;Huang NC;Yen HE
SKD 1（suppressor of K+ transport growth defect 1）是一种AAA型ATP酶，具有分子马达的功能。以前的研究表明，SKD 1积累在表皮膀胱细胞的盐生植物Mesembryocarcinum stack um。SKD 1基因敲除的拟南芥突变体在盐胁迫下表现出Na+/K+比例失衡。两种酶参与蛋白质翻译后修饰，物理相互作用的McSKD 1被确定。McCPN 1（copine 1）是一种RING型泛素连接酶，具有连接至质膜的N-末端肉豆蔻酰化位点、与McSKD 1相互作用的中央copine结构域和催化蛋白质泛素化的C-末端RING结构域。体外泛素化实验表明McCPN 1能够介导McSKD 1的泛素化。McSnRK 1（蔗糖非发酵1-相关蛋白激酶）是一种Ser/Thr蛋白激酶，其含有N-末端STKc催化结构域以磷酸化McSKD 1，以及C-末端乌巴和KA 1结构域以与McSKD 1相互作用。随着NaCl浓度的增加，McSnRK 1的转录水平和蛋白水平均增加。通过酵母三杂交和双分子荧光互补证实了SKD 1-SnRK 1-CPN 1三元复合物的形成。结果发现，McSKD 1优先与McSnRK 1在胞质溶胶中相互作用，盐诱导McSKD 1和McSnRK 1通过微管细胞骨架向质膜重新分布，随后与RING型E3 McCPN 1相互作用。泛素化和磷酸化对McSKD 1的潜在影响，如ATP酶活性和细胞定位的变化，以及它们如何与SKD 1在盐胁迫下维持Na+/K+稳态的功能进行了讨论。
SKD1 (suppressor of K+ transport growth defect 1) is an AAA-type ATPase that functions as a molecular motor. It was previously shown that SKD1 accumulates in epidermal bladder cells of the halophyte Mesembryanthemum crystallinum. SKD1 knock-down Arabidopsis mutants showed an imbalanced Na+/K+ ratio under salt stress. Two enzymes involved in protein post-translational modifications that physically interacted with McSKD1 were identified. McCPN1 (copine 1), a RING-type ubiquitin ligase, has an N-terminal myristoylation site that links to the plasma membrane, a central copine domain that interacts with McSKD1, and a C-terminal RING domain that catalyses protein ubiquitination. In vitro ubiquitination assay demonstrated that McCPN1 was capable of mediating ubiquitination of McSKD1. McSnRK1 (sucrose non-fermenting 1-related protein kinase) is a Ser/Thr protein kinase that contains an N-terminal STKc catalytic domain to phosphorylate McSKD1, and C-terminal UBA and KA1 domains to interact with McSKD1. The transcript and protein levels of McSnRK1 increased as NaCl concentrations increased. The formation of an SKD1–SnRK1–CPN1 ternary complex was demonstrated by yeast three-hybrid and bimolecular fluorescence complementation. It was found that McSKD1 preferentially interacts with McSnRK1 in the cytosol, and salt induced the re-distribution of McSKD1 and McSnRK1 towards the plasma membrane via the microtubule cytoskeleton and subsequently interacted with RING-type E3 McCPN1. The potential effects of ubiquitination and phosphorylation on McSKD1, such as changes in the ATPase activity and cellular localization, and how they relate to the functions of SKD1 in the maintenance of Na+/K+ homeostasis under salt stress, are discussed.
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DOI：
10.1083/jcb.200508166
发表时间：
2006-02-27
期刊：
The Journal of cell biology
影响因子：
--
作者：
Azmi I;Davies B;Dimaano C;Payne J;Eckert D;Babst M;Katzmann DJ
通讯作者：
Katzmann DJ
DOI：
10.1038/nrm2937
发表时间：
2010-08
期刊：
Nature reviews. Molecular cell biology
影响因子：
--
作者：
通讯作者：
--
影响因子：
7.4
作者：
Belin, Christophe;de Franco, Pierre-Olivier;Thomine, Sebastien
通讯作者：
Thomine, Sebastien
影响因子：
2.6
作者：
GIETZ, RD;SCHIESTL, RH;WOODS, RA
通讯作者：
WOODS, RA
影响因子：
6.9
作者：
Agarie, Sakae;Shimoda, Toshifumi;Cushman, John C.
通讯作者：
Cushman, John C.