Summary
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.
