Function and regulation of SUMO proteases

Regulation and function of SUMO modification.

Regulation of Protein Function by SUMO Modification

SUMOylation is a post-translational modification that affects a large number of proteins, many of which are nuclear. While the role of SUMOylation is beginning to be elucidated, it is clear that understanding the mechanisms that regulate the process is likely to be important. Control of the levels of SUMOylation is brought about through a balance of conjugating and deconjugating activities, i.e...

A new class of SUMO proteases.

The small ubiquitin-related modifier (SUMO) is a ubiquitin-like (UBL) protein that can be conjugated to hundreds of different proteins. Such ‘sumoylation’—which is highly dynamic— alters the stability, localization or functional properties of the modified substrate, most often by altering its interactions with other proteins [1,2]. Enzymes known to remove SUMO from substrates, the SUMO protease...

Identification and Developmental Expression of Xenopus laevis SUMO Proteases

SUMO proteins are small ubiquitin-related modifiers. All SUMOs are synthesized as propeptides that are post-translationally cleaved prior to conjugation. After processing, SUMOs become covalently conjugated to cellular targets through a pathway that is similar to ubiquitination. Ubiquitin like protein proteases/Sentrin specific proteases (Ulp/SENPs) mediate both processing and deconjugation of ...

Swapping small ubiquitin-like modifier (SUMO) isoform specificity of SUMO proteases SENP6 and SENP7.

SUMO proteases can regulate the amounts of SUMO-conjugated proteins in the cell by cleaving off the isopeptidic bond between SUMO and the target protein. Of the six members that constitute the human SENP/ULP protease family, SENP6 and SENP7 are the most divergent members in their conserved catalytic domain. The SENP6 and SENP7 subclass displays a clear proteolytic cleavage preference for SUMO2/...