Ubiquitin – Multifaceted Centerline Lights for Biochemical Processes
A special issue of Life (ISSN 2075-1729). This special issue belongs to the section "Biochemistry, Biophysics and Computational Biology".
Deadline for manuscript submissions: closed (15 June 2021) | Viewed by 287
Special Issue Editor
Special Issue Information
Dear Colleagues,
Since the ubiquitin–proteasome system of highly specific protein degradation was first described, the way in which ubiquitin modification participates in it has continuously been investigated . This reversible posttranslational modification of proteins is the basis of several critically important cellular processes, such as protein turnover and sorting, DNA repair and DNA damage response, regulation of cell proliferation, apoptosis, and intracellular signaling. Regarding that, it is not surprising that aberrant or deregulated ubiquitination has been linked to many aspects of cellular transformation with a direct contribution to cancer development and progression. Despite a significant shift in the level of knowledge, which has enabled, among other things, the creation of specific anticancer drugs, a considerable number of fundamental questions remain to be answered. These concern not only ubiquitin modification itself (E1, E2, E3 and deubiquitinase enzymes—types, activities, structures. etc.) but also the processes in which the ubiquitin–proteasome system plays a role or directly controls them. With regard to the abovementioned facts, the ubiquitin–proteasome system is a contemporary, particularly important topic with significant potential for various scientific and clinical fields. The present Special Issue aims at summarizing progress at the level of knowledge of ubiquitin-mediated biochemistry.
Dr. Jan Ševčík
Guest Editor
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Keywords
- ubiqutination
- ubiquitin ligases
- deubiquitinases ubiquitin-binding domains
- protein turnover
- cancer
- protein trafficking
- protein complex assembly
- proteasome
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