TMK4-mediated FIP37 phosphorylation regulates auxin-triggered N6-methyladenosine 6-methyladenosine modification of auxin biosynthetic genes in Arabidopsis
文献类型： 外文期刊
作者： Li, Bin 1 ; Zhou, Qiting 1 ; Cai, Linjun 1 ; Li, Lan 5 ; Xie, Chong 1 ; Li, Donghao 1 ; Zhu, Fan 1 ; Li, Xiushan 1 ; Zhao, Xiaoying 1 ; Liu, Xuanming 1 ; Shen, Lisha 3 ; Xu, Tongda 4 ; He, Chongsheng 1 ;
作者机构： 1.Hunan Univ, Coll Biol, Hunan Key Lab Plant Funct Genom & Dev Regulat, Changsha 410082, Hunan, Peoples R China
2.Hunan Acad Agr Sci, Hunan Hybrid Rice Res Ctr, State Key Lab Hybrid Rice, Changsha 410125, Hunan, Peoples R China
3.Natl Univ Singapore, Temasek Life Sci Lab, Singapore 117604, Singapore
4.Fujian Agr & Forestry Univ, Haixia Inst Sci & Technol, FAFU Joint Ctr, Hort & Metab Biol Ctr, Fuzhou 350002, Fujian, Peoples R China
5.Xiangnan Univ, Sch Pharm, Chenzhou 423000, Hunan, Peoples R China
期刊名称：CELL REPORTS （ 影响因子：7.5； 五年影响因子：8.5 ）
ISSN： 2211-1247
年卷期： 2024 年 43 卷 8 期
页码：
收录情况： SCI
摘要： The dynamics of N 6-methyladenosine (m6A) 6 A) mRNA modification are tightly controlled by the m6A 6 A methyltransferase complex and demethylases. Here, we find that auxin treatment alters m6A 6 A modification on auxin-responsive genes. Mechanically, TRANSMEMBRANE KINASE 4 (TMK4), a component of the auxin signaling pathway, interacts with and phosphorylates FKBP12-INTERACTING PROTEIN 37 (FIP37), a core component of the m6A 6 A methyltransferase complex, in an auxin-dependent manner. Phosphorylation of FIP37 enhances its interaction with RNA, thereby increasing m6A 6 A modification on its target genes, such as NITRILASE 1 (NIT1), NIT1 ), a gene involved in indole-3-acetic acid (IAA) biosynthesis. 1-Naphthalacetic acid (NAA) treatment accelerates the mRNA decay of NIT1, , in a TMK4- and FIP37-dependent manner, which leads to inhibition of auxin biosynthesis. Our findings identify a regulatory mechanism by which auxin modulates m6A 6 A modification through the phosphorylation of FIP37, ultimately affecting mRNA stability and auxin biosynthesis in plants.
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