14-3-3 Regulates 1-Aminocyclopropane-1-Carboxylate Synthase Protein Turnover in Arabidopsis[C][W]
14-3-3 Regulates 1-Aminocyclopropane-1-Carboxylate Synthase Protein Turnover in Arabidopsis[C][W]
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DOI：
10.1105/tpc.113.110106
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发表时间：
2013-03
期刊：
影响因子：
11.6
通讯作者：
G. M. Yoon;J. Kieber
中科院分区：
文献类型：
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作者：
G. M. Yoon;J. Kieber
14-3-3 蛋白在许多细胞过程中发挥作用。在这里，我们证明 14-3-3s 调节参与乙烯生物合成的蛋白质的稳定性。 14-3-3 直接与 ACC 合酶（一种关键的乙烯生物合成酶）和 ETO1/EOLs E3 泛素连接酶相互作用并调节其周转，后者调节 ACS 蛋白周转，从而在调节乙烯生物合成中发挥关键作用。 14-3-3 蛋白是参与多种生理过程的保守磷酸特异性结合蛋白家族。植物具有大型 14-3-3 基因家族，并且已鉴定出许多结合配偶体，但已定义的功能相对较少。在这里，我们证明 14-3-3 蛋白与拟南芥中的多种 1-氨基环丙烷-1-羧酸合酶 (ACS) 亚型相互作用。 ACS 催化植物激素乙烯生物合成中的限速步骤。这种相互作用增加了 ACS 蛋白的稳定性。 14-3-3s 还与 ETHYLENE-OVERPRODUCER1 (ETO1)/ETO1-LIKE (EOL) 相互作用，这是一组三种功能冗余蛋白，它们是 CULLIN-3 E3 泛素连接酶的组成部分，该连接酶靶向 ACS 蛋白的子集，以便被 26S 蛋白酶体快速降解。与 ACS 相比，与 14-3-3 的相互作用会破坏 ETO1/EOL 的稳定性。体内 ETO1/EOL 水平在介导 ACS 蛋白周转中发挥作用，水平升高会导致 ACS 蛋白水平降低。这些研究表明，乙烯生物合成的调节是通过一种机制发生的，在该机制中，14-3-3 蛋白通过 ACS 的直接相互作用和稳定作用以及通过降低针对 ACS 蛋白子集进行降解的泛素连接酶的丰度来发挥作用。
14-3-3 proteins function in many cellular processes. Here, we show that 14-3-3s regulate the stability of proteins involved in ethylene biosynthesis. 14-3-3 directly interacts with and regulates the turnover of ACC synthase, a key ethylene biosynthesis enzyme, and the ETO1/EOLs E3 ubiquitin ligases, which regulate ACS protein turnover, thus playing a key role in regulating ethylene biosynthesis. 14-3-3 proteins are a family of conserved phospho-specific binding proteins involved in diverse physiological processes. Plants have large 14-3-3 gene families, and many binding partners have been identified, though relatively few functions have been defined. Here, we demonstrate that 14-3-3 proteins interact with multiple 1-aminocyclopropane-1-carboxylate synthase (ACS) isoforms in Arabidopsis thaliana. ACS catalyzes the generally rate-limiting step in the biosynthesis of the phytohormone ethylene. This interaction increases the stability of the ACS proteins. 14-3-3s also interact with the ETHYLENE-OVERPRODUCER1 (ETO1)/ETO1-LIKE (EOLs), a group of three functionally redundant proteins that are components of a CULLIN-3 E3 ubiquitin ligase that target a subset of the ACS proteins for rapid degradation by the 26S proteasome. In contrast with ACS, the interaction with 14-3-3 destabilizes the ETO1/EOLs. The level of the ETO1/EOLs in vivo plays a role in mediating ACS protein turnover, with increased levels leading to a decrease in ACS protein levels. These studies demonstrate that regulation of ethylene biosynthesis occurs by a mechanism in which 14-3-3 proteins act through a direct interaction and stabilization of ACS and through decreasing the abundance of the ubiquitin ligases that target a subset of ACS proteins for degradation.