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Article Dans Une Revue Postepy Biologii Komorki Année : 2021

THE MANY FACES OF UBIQUITINATION

Résumé

Ubiquitination is a post-translational modification of proteins that plays an essential role in regulating many cellular processes. Defects in this control mechanism are associated with various diseases, including cancer, neurodegenerative and metabolic disorders, muscular atrophies, or viral infections. In this process, one of the key regulatory proteins - ubiquitin (Ub) marks improperly structured, or non-functioning proteins. These are then degraded by the proteasome. The attachment of ubiquitin to the substrate proteins can also have other important functional consequences for the cell. It is now known that ubiquitination of a particular substrate protein may affect its localization in subcellular compartments, influence its interactions with other proteins or regulate its activity. To control protein activity, interactions, localization and degradation, ubiquitin encodes complex molecular signals. It is aided by an extensive network of structurally-related enzymes, namely ubiquitin activating enzymes (E1), ubiquitin conjugating enzymes (E2) and ubiquitin ligases (E3). These enzymes work in concert to regulate the activity and function of other proteins. The studies of the ubiquitination process are important not only to better understand molecular and cellular mechanisms but also for the development of new drugs targeting particular ubiquitin-proteasome system components. This work presents the recent advancements in the field of protein ubiquitination with an emphasis put on various functions that this process may have in the cell.
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Dates et versions

hal-03665064 , version 1 (11-05-2022)

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  • HAL Id : hal-03665064 , version 1

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Natalia Lazarewicz, Ewa Blaszczak. THE MANY FACES OF UBIQUITINATION. Postepy Biologii Komorki, 2021, 48 (3), pp.197-216. ⟨hal-03665064⟩
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