Ubiquitination in Health and Disease
A special issue of Cells (ISSN 2073-4409).
Deadline for manuscript submissions: closed (31 December 2018) | Viewed by 70554
Special Issue Editors
Interests: genetic diseases; TRIM E3 ubiquitin ligases; ubiquitination
Special Issues, Collections and Topics in MDPI journals
Interests: medical genetics; epigenetics; chromatinopathies; disease discovery; TRIM proteins
Special Issues, Collections and Topics in MDPI journals
Special Issue Information
Dear Colleagues,
Ubiquitination is a post-translational modification process that controls the degradation, signaling and activity of many, if not all, cellular proteins. Ubiquitination needs to be finely tuned and is catalyzed and controlled by several players: ubiquitin; the E1 ubiquitin activating enzyme, the E2 ubiquitin conjugating enzymes, the E3 ubiquitin ligases, which compose the ubiquitination cascade; the deubiquitination enzymes that reverse the modification; and the proteins that recognize the ubiquitination code and translate the signal. Substrates can be modified with a single ubiquitin peptide, in one or multiple sites, or with a poly-ubiquitin chain. The topology of the built ubiquitin chain determines the fate of the targeted substrate. In cells also free poly-ubiquitin chains, which are not conjugated to any target protein, can be synthesized. In recent years, considerable progress has been made in the understanding the molecular action of ubiquitin in signaling pathways and how alterations in the ubiquitin system lead to the development of several human diseases from cancer, metabolic syndromes, neurodegenerative diseases, inflammatory disorders, and rare genetic disorders.
In this Special Issue of Cells, we invite your contributions, either in the form of original research articles or reviews addressing the expanding field of mechanistic and functional insights into the physiological and pathological role of specific ubiquitination pathways and components.
Prof. Germana MeroniDr. Giuseppe Merla
Guest Editors
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Keywords
- ubiquitin
- E3 ubiquitin ligases
- proteasome
- E2 ubiquitin conjugating enzymes
- ubiquitin binding domains
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