SUMOylation of Proteins and Amino Acid Residues
The SUMOylation of proteins is a post-translational modification wherein Small Ubiquitin-like Modifier (SUMO) proteins are covalently attached to specific amino acid residues of substrate proteins, modulating their function and fate.
Amino Acid Residues
The canonical SUMOylation site consists of a tetrapeptide motif denoted as ψKXE, where ψ represents a hydrophobic residue, K is lysine, X is any amino acid, and E is glutamic acid. In this motif, SUMO is conjugated to the ε-amino group of the lysine residue through an isopeptide bond with its C-terminal glycine.
SUMOylation Process
The SUMOylation of proteins is mediated by a conserved enzymatic cascade that proceeds through three sequential steps: activation, conjugation, and ligation. In the activation phase, the E1 SUMO-activating enzyme catalyzes the formation of a high-energy thioester bond between SUMO and ATP. The activated SUMO is subsequently transferred to the E2 conjugating enzyme. In the final step, the E3 SUMO ligase facilitates the covalent attachment of SUMO to the ε-amino group of the target lysine residue. While the ψKXE motif represents the predominant SUMOylation site, a variety of non-canonical sequences have also been identified as valid modification motifs, expanding the potential substrate repertoire.
Function
SUMOylation of proteins regulates a wide array of cellular processes, including protein stability, nuclear-cytoplasmic transport, transcriptional regulation, DNA repair, and signal transduction. Dysregulation of SUMOylation has been implicated in the pathogenesis of various disorders such as cancer, neurodegenerative diseases, and cardiovascular conditions.
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