The Arabidopsis F-box E3 ligase RIFP1 plays a negative role in abscisic acid signalling by facilitating ABA receptor RCAR3 degradation
The Arabidopsis F-box E3 ligase RIFP1 plays a negative role in abscisic acid signalling by facilitating ABA receptor RCAR3 degradation
复制标题
拟南芥 F-box E3 连接酶 RIFP1 通过促进 ABA 受体 RCAR3 降解，在脱落酸信号传导中发挥负面作用
DOI：
10.1111/pce.12639
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发表时间：
2016-03-01
影响因子：
7.3
通讯作者：
Yang, Yi
中科院分区：
文献类型：
--
作者：
Li, Ying;Zhang, Liang;Yang, Yi
植物激素脱落酸（ABA）在植物生长和发育中起着至关重要的作用。 ABA 的功能由一组新发现的 ABA 受体介导，称为 PYRABACTIN RESISTANCE 1/PYR-LIKE/ABA 受体调节成分 (PYR1/PYLs/RCARs)。在这里，我们报道了拟南芥 F-box 蛋白 RCAR3 相互作用 F-BOX 蛋白 1 (RIFP1) 在体外和体内与 ABA 受体 (RCAR3) 和 SCF E3 连接酶复合物亚基拟南芥 SKP1 样蛋白 (ASK) 相互作用。 rifp1 突变植物表现出 ABA 介导的对种子萌发和离体叶片失水的抑制作用增强，而拟南芥中 RIFP1 的过度表达导致植物对 ABA 不敏感。同时，rifp1突变体植物表现出更强的缺水耐受性。此外，RCAR3蛋白水平在rifp1突变体植物中比野生型植物中更稳定，表明RIFP1促进RCAR3的蛋白酶体降解。因此，RIFP1 的缺失增加了几个 ABA 响应基因的转录水平。综上所述，这些数据表明 RIFP1 在 RCAR3 介导的 ABA 信号通路中发挥负面作用，并可能作为 SCF 泛素连接酶复合物的接头亚基发挥作用，以调节 ABA 受体 RCAR3 的稳定性。 在这份手稿中，鉴定了编码 F-box 蛋白 RCAR3 相互作用 F-BOX 蛋白 1 (RIFP1) 的拟南芥基因。 RIFP1 在体外和体内与 ABA 受体 (RCAR3) 和 SCF E3 连接酶复合物亚基 ASK 相互作用。我们的分析表明，RCAR3 蛋白水平在 rifp1 突变体植物中比野生型植物中更稳定，表明 RIFP1 促进 RCAR3 的蛋白酶体降解。 rifp1 T-DNA 突变体和转基因 RIFP1 过表达植物的 ABA 相关表型也表明 RIFP1 在 RCAR3 介导的 ABA 级联中发挥负面作用。因此，RIFP1 可能作为 SCF 泛素连接酶复合物的接头亚基发挥作用，调节 ABA 受体 RCAR3 的稳定性。
The phytohormone abscisic acid (ABA) plays a vital role in plant growth and development. The function of ABA is mediated by a group of newly discovered ABA receptors, named PYRABACTIN RESISTANCE 1/PYR-LIKE/REGULATORY COMPONENTS OF ABA RECEPTORs (PYR1/PYLs/RCARs). Here, we report that an Arabidopsis thaliana F-box protein RCAR3 INTERACTING F-BOX PROTEIN 1 (RIFP1) interacts with ABA receptor (RCAR3) and SCF E3 ligase complex subunits Arabidopsis SKP1-LIKE PROTEINs (ASKs) in vitro and in vivo. The rifp1 mutant plants displayed increased ABA-mediated inhibition of seed germination and water loss of detached leaves, while the overexpression of RIFP1 in Arabidopsis led to plants being insensitive to ABA. Meanwhile, the rifp1 mutant plants showed greater tolerance to water deficit. In addition, the RCAR3 protein level was more stable in the rifp1 mutant plants than in the wild-type plants, indicating that RIFP1 facilitates the proteasome degradation of RCAR3. Accordingly, the loss of RIFP1 increased the transcript levels of several ABA-responsive genes. Taken together, these data indicate that RIFP1 plays a negative role in the RCAR3-mediated ABA signalling pathway and likely functions as an adaptor subunit of the SCF ubiquitin ligase complex to regulate ABA receptor RCAR3 stability.In this manuscript, an Arabidopsis gene encodes an F-box protein RCAR3 INTERACTING F-BOX PROTEIN 1 (RIFP1) was identified. RIFP1 interacted with ABA receptor (RCAR3) and SCF E3 ligase complex subunits ASKs in vitro and in vivo. Our analysis indicated that RCAR3 protein level was more stable in the rifp1 mutant plants than that in the wild type plants, indicating that RIFP1 facilitates the proteasome degradation of RCAR3. The ABA related phenotypes of rifp1 T-DNA mutant and transgenic RIFP1-overexpression plants also indicated that RIFP1 plays a negative role in the RCAR3 mediated ABA cascade. Hence, RIFP1 likely functions as an adaptor subunit of SCF ubiquitin ligase complex to regulate ABA receptor RCAR3 stability.