Unveiling the Roles of SUMO Proteases in Plants During Abiotic Stress

Plants adapt to changing environments by evolving distinctive mechanisms like post-translational modification (PTM) of proteins such as ubiquitination and SUMOylation. PTMs can impact protein interactions, stability, and cellular or sub-cellular localization, thereby introducing added complexity by altering proteins. In plants, the SUMOylation pathway plays a significant role in responding to environmental stimuli such as heat, cold, drought, and salt stresses. Ubiquitination and SUMOylation have a similar process of activating, conjugating, and attaching modifiers to the target protein. However, unlike SUMO, the ubiquitin pathway boasts a wide array of enzymes for specificity. The SUMO system has a limited number of ligases even in fully sequenced plant genomes. Current studies have emphasized the SUMO proteases, especially the ubiquitin-like protease (ULPs), which play roles in detaching SUMO from its substrate. Research on SUMO proteases indicates that the enzymatic removal of SUMO from its substrate by these active proteases is a vital aspect of the SUMO system. This review paper delves into the roles of ULPs in stress responses, highlighting the crucial balance between promoting growth and managing stress by fine-tuning SUMO attachment and removal.