Protein ubiquitination is a post-translational modification that entails the covalent attachment of the small protein ubiquitin (Ub), which acts as a signal to direct protein stability, localization, or interactions. The Ub code is written by a family of enzymes called E3 Ub ligases (∼600 members in humans), which can catalyze the transfer of either a single ubiquitin or the formation of a diverse array of polyubiquitin chains. This code can be edited or erased by a different set of enzymes termed deubiquitinases (DUBs; ∼100 members in humans). While enzymes from these distinct families have seemingly opposing activities, certain E3–DUB pairings can also synergize to regulate vital cellular processes like gene expression, autophagy, innate immunity, and cell proliferation. In this review, we highlight recent studies describing Ub ligase-DUB interactions and focus on their relationships.
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Cover Image
Cover Image
Gas vesicles are protein megacomplexes filled with gas to allow aquatic bacteria to control their vertical position in the water column. The cover image shows a detailed model of a complete gas vesicle. The model is deposited and made publicly available in a data repository (zenodo.org/record/6458345). Besides the striking geometry of the structure, the image also highlights the function of gas vesicles as buoyancy devices (filled with yellow gas) and the gas-permeability of the wall (with yellow gas molecules diffusing around). For more information, see the article by Huber and Jakobi (pp. 205–215) in this issue. Image provided by Arjen Jakobi.
Friend or foe? Reciprocal regulation between E3 ubiquitin ligases and deubiquitinases
Derek L. Bolhuis, Michael J. Emanuele, Nicholas G. Brown; Friend or foe? Reciprocal regulation between E3 ubiquitin ligases and deubiquitinases. Biochem Soc Trans 28 February 2024; 52 (1): 241–267. doi: https://doi.org/10.1042/BST20230454
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