SUMOrelated

SUMO-related refers to the cellular and molecular processes that involve SUMOylation, a reversible post-translational modification in which small ubiquitin-like modifier (SUMO) proteins are covalently attached to lysine residues on target proteins. SUMOylation affects protein activity, interactions, localization, and stability, and it participates in numerous cellular pathways.

In humans, the SUMO family includes SUMO-1 and SUMO-2/3, with SUMO-2/3 capable of forming polySUMO chains and responding to cellular stress, while SUMO-1 is more constitutively expressed. SUMOylation proceeds through a hierarchical enzymatic cascade: an E1 activating enzyme (SAE1/SAE2) initiates activation, UBC9 (the E2 conjugating enzyme) transfers SUMO, and E3 ligases such as the PIAS family or RanBP2 provide substrate specificity. Removal is carried out by SENP proteases, restoring the unmodified state. Substrate selection and efficiency are influenced by SUMO-interacting motifs on targets and by cellular context.

SUMO modifications regulate transcription factors, chromatin structure, DNA damage response, protein stability, and signaling pathways. They influence nuclear transport, spindle assembly, and stress responses. SUMOylation is typically dynamic and context-dependent, with stimuli such as heat shock, DNA damage, or oxidative stress altering SUMO conjugation patterns.

Because SUMOylation affects a broad set of proteins, disruptions are studied in relation to cancer, neurodegenerative disease, and cardiovascular disorders in some contexts. Researchers map substrates and enzymes through proteomics, SUMO-remnant profiling, and genetic models, while therapeutic strategies seek to modulate SUMOylation, acknowledging challenges in specificity and safety.

Related concepts include SUMO-interacting motifs (SIMs) and polySUMO chains, and cross-regulation with ubiquitin pathways. The field continues to broaden the catalog of SUMO substrates and the biological contexts in which SUMO-related regulation is decisive.