SUMOmodified

SUMOmodified is a term used in molecular biology to describe a protein that has undergone SUMOylation. SUMOylation is a post-translational modification process where a small ubiquitin-like modifier (SUMO) protein is covalently attached to a target protein. This modification is reversible and plays a crucial role in regulating a wide array of cellular processes.

The SUMOylation process involves a series of enzymatic steps, typically carried out by an E1 activating enzyme, an E2 conjugating enzyme, and an E3 ligase. The SUMO protein is first activated by the E1 enzyme, then transferred to the E2 enzyme, and finally, with the help of an E3 ligase, it is attached to a lysine residue on the target protein. This process is analogous to ubiquitination but serves different cellular functions.

SUMOmodified proteins can exhibit altered functional properties compared to their unmodified counterparts. SUMOylation can influence protein localization within the cell, protein-protein interactions, DNA binding activity, and protein stability. It is involved in regulating transcription, DNA repair, signal transduction, and the immune response, among other cellular functions. The specific effects of SUMOylation are dependent on the target protein and the site of modification. De-SUMOylation, the removal of SUMO, is carried out by specific proteases, ensuring the dynamic regulation of SUMOylated proteins. Aberrant SUMOylation has been linked to various diseases, including cancer and neurodegenerative disorders, highlighting its importance in cellular homeostasis.