磷酸化
基因敲除
激酶
细胞生物学
拟南芥
蛋白酶体
脱磷
突变体
小RNA
生物
拟南芥
化学
生物化学
磷酸酶
基因
作者
Lin Wang,Xingxing Yan,Yanjun Li,Zhiye Wang,Shweta Chhajed,Baoshuan Shang,Zhen Wang,Sukwon Choi,Hongwei Zhao,Sixue Chen,Xiuren Zhang
出处
期刊:Science Advances
[American Association for the Advancement of Science (AAAS)]
日期:2022-03-25
卷期号:8 (12)
被引量:16
标识
DOI:10.1126/sciadv.abm8435
摘要
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.
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