| Small ubiquitin-like modification (SUMOylation) is a crucial post-translational modification of proteins that plays a vital role in various biological processes in plants. This modification involves the covalent attachment of SUMO proteins to target proteins, thereby influencing their function and activity. Multiple enzymes are involved in this process, including SUMO-specific proteases, SUMO activating enzymes, SUMO conjugating enzymes, and SUMO ligases.There are multiple SUMO proteins and enzymes in plants, and each possesses distinct structural and functional characteristics. However, the precise relationship between different SUMO proteins and the specific enzyme combinations involved in the modification process has not been clarified completely. Therefore, it is of utmost importance to elucidate the characteristics of these SUMO proteins and enzymes to facilitate further researches. Another challenge lies in the identification of SUMOylation substrates. Methods such as mass spectrometry and yeast two-hybrid are available for substrate identification; however, there was still limitations, particularly in crops like maize. Consequently, the development of additional identification methods is necessary to recognize SUMOylation substrates and uncover the mechanisms underlying SUMOylation in maize growth, development and stress responses. To advance the research on SUMOylation, this review aims to provide a comprehensive summary of SUMO proteins, SUMOylation-related enzymes, protein SUMOylation process, identification methods for substrates, and the research
progress in maize protein SUMOylation. By comprehending the regular patterns of SUMOylation and current research techniques, it will offer valuable guidance for maize breeding and researches of other plants and help related researches to have a deeper understanding of the response patterns of SUMOylation in plant growth, development and stress responses. |
