Domains in Action: Understanding Ddi1’s Diverse Functions in the Ubiquitin-Proteasome System
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Le résumé fourni par la source
The ubiquitin-proteasome system (UPS) is a pivotal cellular mechanism responsible for the selective degradation of proteins, playing an essential role in proteostasis, protein quality control, and regulating various cellular processes, with ubiquitin marking proteins for degradation through a complex, multi-stage process. The shuttle proteins family is a very unique group of proteins that plays an important role in the ubiquitin-proteasome system. Ddi1, Dsk2, and Rad23 are shuttle factors that bind ubiquitinated substrates and deliver them to the 26S proteasome. Besides mediating the delivery of ubiquitinated proteins, they are also involved in many other biological processes. Ddi1, the least-studied shuttle protein, exhibits unique physicochemical properties that allow it to play non-canonical functions in the cells. It regulates cell cycle progression and response to proteasome inhibition and defines MAT type of yeast cells. The Ddi1 contains UBL and UBA domains, which are crucial for binding to proteasome receptors and ubiquitin respectively, but also an additional domain called RVP. Additionally, much evidence has been provided to question whether Ddi1 is a classical shuttle protein. For many years, the true nature of this protein remained unclear. Here, we highlight the recent discoveries, which shed new light on the structure and biological functions of the Ddi1 protein.
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Le contrôle bibliographique ouvert
DOI retrouvé dans Crossref DOI retrouvé ; titre concordant.
- Titre Crossref
- Domains in Action: Understanding Ddi1’s Diverse Functions in the Ubiquitin-Proteasome System
- Date Crossref
- 06/04/2024
- Éditeur
- MDPI AG
- Type
- journal-article
Ce recoupement confirme des métadonnées liées au DOI. Il ne confirme ni la méthode ni les conclusions de l’étude, et il ne compte pas comme une seconde source scientifique indépendante.
Où se fait cette recherche
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Polish Mother’s Memorial Hospital Research Institute Department of Neurosurgery pays non établi dans la noticeÉtablissement de santé
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Medical University of Lodz Department of Medical Biochemistry pays non établi dans la noticeUniversité ou école supérieure
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Medical University of Warsaw pays non établi dans la noticeUniversité ou école supérieure
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Faculty of Health Sciences Department of Rehabilitation Medicine pays non établi dans la noticeUniversité ou école supérieure
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Faculty of Dental Medicine Department of Rehabilitation pays non établi dans la noticeUniversité ou école supérieure
Department of Neurosurgery — Polish Mother’s Memorial Hospital Research Institute, Department of Medical Biochemistry — Medical University of Lodz et Medical University of Warsaw, avec 2 autres affiliations.
Une affiliation ne permet pas de déduire la nationalité d’un auteur.