Liu Wei, Jenkins Gareth I
School of Molecular Biosciences, College of Medical, Veterinary and Life Sciences, Bower Building, University of Glasgow, Glasgow G12 8QQ, UK.
J Exp Bot. 2025 Feb 7;76(3):873-881. doi: 10.1093/jxb/erae132.
The UV RESISTANCE LOCUS 8 (UVR8) photoreceptor mediates many plant responses to UV-B and short wavelength UV-A light. UVR8 functions through interactions with other proteins which lead to extensive changes in gene expression. Interactions with particular proteins determine the nature of the response to UV-B. It is therefore important to understand the molecular basis of these interactions: how are different proteins able to bind to UVR8 and how is differential binding regulated? This concise review highlights recent developments in addressing these questions. Key advances are discussed with regard to: identification of proteins that interact with UVR8; the mechanism of UVR8 accumulation in the nucleus; the photoactivation of UVR8 monomer; the structural basis of interaction between UVR8 and CONSTITUTIVELY PHOTOMORPHOGENIC 1 (COP1) and REPRESSOR OF UV-B PHOTOMORPHOGENESIS (RUP) proteins; and the role of UVR8 phosphorylation in modulating interactions and responses to UV-B. Nevertheless, much remains to be understood, and the need to extend future research to the growing list of interactors is emphasized.
紫外线抗性位点8（UVR8）光感受器介导了植物对UV-B和短波长UV-A光的多种反应。UVR8通过与其他蛋白质相互作用发挥功能，这些相互作用导致基因表达发生广泛变化。与特定蛋白质的相互作用决定了对UV-B反应的性质。因此，了解这些相互作用的分子基础很重要：不同蛋白质如何能够与UVR8结合，以及差异结合是如何被调控的？这篇简要综述突出了在解决这些问题方面的最新进展。讨论了在以下方面取得的关键进展：与UVR8相互作用的蛋白质的鉴定；UVR8在细胞核中积累的机制；UVR8单体的光激活；UVR8与组成型光形态建成1（COP1）和UV-B光形态建成抑制因子（RUP）蛋白质之间相互作用的结构基础；以及UVR8磷酸化在调节对UV-B的相互作用和反应中的作用。然而，仍有许多有待了解的地方，并强调需要将未来的研究扩展到越来越多的相互作用蛋白。
