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. 2024 Jul 29;17:1446686. doi: 10.3389/fnmol.2024.1446686

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Copyright © 2024 van der Laan, ten Voorde, Mannens and Henneman.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Overview of the ubiquitination pathway: Ubiquitin (ub) is attached to an E1 activating enzyme following ATP hydrolysis. Subsequently, ub is transferred to the E2 conjugating enzyme, and then the E3 ligase facilitates the transfer of ub from E2 to the target protein. Deubiquitinases (DUBs) are responsible for removing ubiquitin molecules from the target protein. The type (mono-, poly-) and the site of ubiquitination exert distinct effects on the fate of the target protein. Ubiquitination can serve as: (1) a marker for proteasomal degradation, (2) a modifier of protein interactions, or (3) a determinant of cellular localization (Created with BioRender).