From the ‡Department of Genetics, Development and Cell Biology, Iowa State University, Ames, IA 50011.
Mol Cell Proteomics. 2018 Jun;17(6):1047-1054. doi: 10.1074/mcp.MR117.000476. Epub 2018 Mar 7.
Ubiquitin-mediated control of protein stability is central to most aspects of plant hormone signaling. Attachment of ubiquitin to target proteins occurs via an enzymatic cascade with the final step being catalyzed by a family of enzymes known as E3 ubiquitin ligases, which have been classified based on their protein domains and structures. Although E3 ubiquitin ligases are conserved among eukaryotes, in plants they are well-known to fulfill unique roles as central regulators of phytohormone signaling, including hormone perception and regulation of hormone biosynthesis. This review will highlight up-to-date findings that have refined well-known E3 ligase-substrate interactions and defined novel E3 ligase substrates that mediate numerous hormone signaling pathways. Additionally, examples of how particular E3 ligases may mediate hormone crosstalk will be discussed as an emerging theme. Looking forward, promising experimental approaches and methods that will provide deeper mechanistic insight into the roles of E3 ubiquitin ligases in plants will be considered.
泛素介导的蛋白质稳定性控制是植物激素信号转导的大多数方面的核心。通过酶级联反应将泛素附着到靶蛋白上,最后一步由称为 E3 泛素连接酶的酶家族催化,这些酶根据其蛋白质结构域和结构进行分类。尽管 E3 泛素连接酶在真核生物中是保守的,但在植物中,它们作为植物激素信号转导的中央调节剂发挥着独特的作用,包括激素感知和激素生物合成的调节。这篇综述将重点介绍最新的发现,这些发现完善了众所周知的 E3 连接酶-底物相互作用,并确定了介导众多激素信号通路的新型 E3 连接酶底物。此外,还将讨论特定 E3 连接酶如何介导激素串扰,这是一个新兴的主题。展望未来,将考虑有前途的实验方法和技术,为 E3 泛素连接酶在植物中的作用提供更深入的机制见解。