PRP4KA phosphorylates SERRATE for degradation via 20S proteasome to fine-tune miRNA production in Arabidopsis.

PRP4KA phosphorylates SERRATE for degradation via 20S proteasome to fine-tune miRNA production in Arabidopsis.
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DOI:
10.1126/sciadv.abm8435
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发表时间:
2022-03-25
期刊:
影响因子:
13.6
通讯作者:
Zhang X
Zhang X
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Wang L;Yan X;Li Y;Wang Z;Chhajed S;Shang B;Wang Z;Choi SW;Zhao H;Chen S;Zhang X

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磷酸化可以快速地打开/关闭蛋白质功能。本文报道了前mRNA加工4激酶A(PRP 4KA)及其同源物与RNA加工中的关键因子锯齿(SE)的相互作用。PRP 4KA在体外和体内至少磷酸化5个SE残基。低磷酸化而非高磷酸化的SE变异体可在体内容易地拯救se表型。此外,低磷酸化的SE变体与微处理器组分HYL 1的结合亲和力更强,并且比高磷酸化的对应物更能抵抗20 S蛋白酶体的降解。敲低激酶增强了低磷酸化SE的积累。然而,过量的硒干扰了以硒为支架的大分子复合物的组装和功能,导致突变体和野生型背景中出现硒样缺陷。因此,通过PRP 4KA磷酸化SE可以快速清除积累的SE,以确保其适当的量。本研究为蛋白质磷酸化如何通过调控植物体内SE积累的动态平衡来调控miRNA代谢提供了新的视角。PRP 4KA介导的磷酸化标记Serrate/Ars 2用于降解20 S蛋白酶体以控制植物中的miRNA加工
Phosphorylation can quickly switch on/off protein functions. Here, we reported pre-mRNA processing 4 kinase A (PRP4KA), and its paralogs interact with Serrate (SE), a key factor in RNA processing. PRP4KA phosphorylates at least five residues of SE in vitro and in vivo. Hypophosphorylated, but not hyperphosphorylated, SE variants could readily rescue se phenotypes in vivo. Moreover, hypophosphorylated SE variants had stronger binding affinity to microprocessor component HYL1 and were more resistant to degradation by 20S proteasome than hyperphosphorylated counterparts. Knockdown of the kinases enhanced the accumulation of hypophosphorylated SE. However, the excessive SE interfered with the assembly and function of SE-scaffolded macromolecule complexes, causing the se-like defects in the mutant and wild-type backgrounds. Thus, phosphorylation of SE via PRP4KA can quickly clear accumulated SE to secure its proper amount. This study provides new insight into how protein phosphorylation regulates miRNA metabolism through controlling homeostasis of SE accumulation in plants. PRP4KA-mediated phosphorylation tags Serrate/Ars2 for degradation versus 20S proteasome to control miRNA processing in plants.
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