AI Article Synopsis
- SUMOylation involves the addition of small ubiquitin-like modifiers to proteins, helping regulate key nuclear functions.
- The process is controlled through a series of enzymes and can be reversed by SUMO-specific proteases (SENPs), with imbalances linked to diseases like cancer.
- Recent research has focused on SENPs as potential drug targets, discussing inhibitors and methods for assessing their activity in the development of therapies.
Article Abstract
SUMOylation is a reversible and highly dynamic post-translational modification of target proteins by small ubiquitin-like modifiers (SUMO). It is orchestrated by SUMO-activating, -conjugating, and -ligating enzymes in a sequential manner and is important in regulating a myriad of predominantly nuclear processes. DeSUMOylation is achieved by SUMO-specific proteases (SENPs). Deregulation of SUMOylation and deSUMOylation results in cellular dysfunction and is linked to various diseases, including cancer. In recent years, SENPs have emerged as potential therapeutic targets. In this review, we will describe the inhibitors and activity-based probes of SENPs. Furthermore, we will summarize the biochemical assays available for evaluating the activity of SENPs to identify inhibitors.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6862319 | PMC |
| http://dx.doi.org/10.1021/acschembio.9b00402 | DOI Listing |
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