AI Article Synopsis
- Small ubiquitin-like modifier (SUMO)-targeted E3 ubiquitin ligases (STUbLs) are enzymes that add ubiquitin to proteins that have been modified by SUMO, linking the processes of SUMOylation and ubiquitination in cells.
- STUbLs play essential roles in various cell cycle events, such as DNA repair, replication, and mitosis, and can respond to stress from DNA damage.
- They often function in specific locations within the cell, like the nuclear envelope, to help correctly reposition damaged DNA or stalled replication processes, thereby supporting genome stability.
Article Abstract
Small ubiquitin-like modifier (SUMO)-targeted E3 ubiquitin ligases (STUbLs) are specialized enzymes that recognize SUMOylated proteins and attach ubiquitin to them. They therefore connect the cellular SUMOylation and ubiquitination circuits. STUbLs participate in diverse molecular processes that span cell cycle regulated events, including DNA repair, replication, mitosis, and transcription. They operate during unperturbed conditions and in response to challenges, such as genotoxic stress. These E3 ubiquitin ligases modify their target substrates by catalyzing ubiquitin chains that form different linkages, resulting in proteolytic or non-proteolytic outcomes. Often, STUbLs function in compartmentalized environments, such as the nuclear envelope or kinetochore, and actively aid in nuclear relocalization of damaged DNA and stalled replication forks to promote DNA repair or fork restart. Furthermore, STUbLs reside in the same vicinity as SUMO proteases and deubiquitinases (DUBs), providing spatiotemporal control of their targets. In this review, we focus on the molecular mechanisms by which STUbLs help to maintain genome stability across different species.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8161396 | PMC |
| http://dx.doi.org/10.3390/ijms22105391 | DOI Listing |
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