Ingole Kishor D, Alekseeva Elizaveta, Lilley Kathryn S, Sadanandom Ari
Department of Biochemistry, University of Cambridge, Cambridge, CB2 1RX, UK.
Department of Biosciences, Durham University, Durham, DH1 3LE, UK.
New Phytol. 2025 Jul;247(1):90-96. doi: 10.1111/nph.70176. Epub 2025 May 6.
Protein posttranslational modifications (PTMs) are vital for regulating protein functions. SUMOylation, a PTM essential for plant survival, involves attaching a Small Ubiquitin-like MOdifier (SUMO) to lysine residues of target proteins. SUMOylation influences stress tolerance, cell proliferation, protein stability, and gene expression. While well studied in mammals and yeast, SUMOylation studies in plants are scarce, as the identification of SUMOylated proteins and the specific modification sites is challenging. Deciphering the plant SUMOylome is essential for understanding stress response mechanisms. Advanced proteomic techniques are necessary to map these complex protein modifications. This article offers insights into the workflows employed for probing the SUMOylome. We analyze how current technological approaches have advanced our understanding of SUMOylation and highlight limitations that currently impede comprehensive mapping of SUMO signaling pathways.
蛋白质翻译后修饰（PTM）对于调节蛋白质功能至关重要。SUMO化是植物生存所必需的一种PTM，它涉及将一个小泛素样修饰物（SUMO）连接到靶蛋白的赖氨酸残基上。SUMO化影响胁迫耐受性、细胞增殖、蛋白质稳定性和基因表达。虽然在哺乳动物和酵母中对SUMO化已有充分研究，但在植物中的SUMO化研究却很少，因为鉴定SUMO化蛋白和特定修饰位点具有挑战性。解析植物SUMO化蛋白质组对于理解胁迫反应机制至关重要。先进的蛋白质组学技术对于绘制这些复杂的蛋白质修饰图谱是必要的。本文深入探讨了用于探测SUMO化蛋白质组的工作流程。我们分析了当前的技术方法如何增进了我们对SUMO化的理解，并突出了目前阻碍全面绘制SUMO信号通路图谱的局限性。
