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Topic Review
Ubiquitylation
Ubiquitylation is a post-translational modification that covalently conjugates the ubiquitin molecule through the C-terminus to a lysine residue on a substrate protein. Ubiquitylation results in the turnover of the ubiquitylated substrate protein by either the proteasome or lysosome, a change in subcellular localization of the substrate protein, or alteration of substrate protein function . Ubiquitylation is mediated by three enzymes and scaffolding proteins: E1, E2, and E3.
  • 818
  • 22 Jun 2021
Topic Review
Ubiquitination System
Ubiquitination of proteins, like phosphorylation and acetylation, is an important regulatory aspect influencing numerous and various cell processes, such as immune response signaling and autophagy. The study of ubiquitination has become essential to learning about host–pathogen interactions, and a better understanding of the detailed mechanisms through which pathogens affect ubiquitination processes in host cell will contribute to vaccine development and effective treatment of diseases. 
  • 726
  • 30 Mar 2021
Topic Review
Ubiquitination of ETS Transcription Factors
Genome expansion, whole genome and gene duplication events during metazoan evolution produced an extensive family of ETS genes whose members express transcription factors with a conserved winged helix-turn-helix DNA-binding domain. Key determinants of the cellular repertoire of ETS proteins are their stability and turnover, controlled largely by the actions of selective E3 ubiquitin ligases and deubiquitinases. Here we discuss the known relationships between ETS proteins and enzymes that determine their ubiquitin status, their integration with other developmental signal transduction pathways and how suppression of ETS protein ubiquitination contributes to the malignant cell phenotype in multiple cancers.
  • 769
  • 21 Jul 2021
Topic Review
Ubiquitination in ABA Signaling
The plant hormone abscisic acid (ABA) rapidly accumulates in plants in response to environmental stress and plays a pivotal role in the reaction to various stimuli. Increasing evidence demonstrates a significant role of ubiquitination and subsequent selective degradation in controlling ABA signaling. We present updated information on the components of the ABA signaling pathway modified by different E3 ligases.
  • 533
  • 11 May 2021
Topic Review
Ubiquitin-Specific Peptidase (USP) Inhibitors
Ubiquitylation and deubiquitylation are reversible protein post-translational modification (PTM) processes involving the regulation of protein degradation under physiological conditions. Loss of balance in this regulatory system can lead to a wide range of diseases, such as cancer and inflammation. As the main members of the deubiquitinases (DUBs) family, ubiquitin-specific peptidases (USPs) are closely related to biological processes through a variety of molecular signaling pathways, including DNA damage repair, p53 and transforming growth factor-β (TGF-β) pathways.
  • 1.6K
  • 11 Jun 2021
Topic Review
Ubiquitin-Proteasome System in Spermatogenesis
Spermatogenesis is a prolonged and highly ordered physiological process that produces haploid male germ cells through more than 40 steps and experiences dramatic morphological and cellular transformations. The ubiquitin proteasome system (UPS) plays central roles in the precise control of protein homeostasis to ensure the effectiveness of certain protein groups at a given stage and the inactivation of them after this stage. Many UPS components have been demonstrated to regulate the progression of spermatogenesis at different levels. Especially in recent years, novel testis-specific proteasome isoforms have been identified to be essential and unique for spermatogenesis. 
  • 498
  • 08 Apr 2022
Topic Review
Ubiquitin-Proteasome System
Kidney transplantation is the preferred treatment for end-stage kidney disease (ESKD). Compared to maintenance dialysis, kidney transplantation results in improved patient survival and quality of life. Kidneys from living donors perform best; however, many patients with ESKD depend on kidneys from deceased donors. After procurement, donor kidneys are placed in a cold-storage solution until a suitable recipient is located. Sadly, prolonged cold storage times are associated with inferior transplant outcomes; therefore, in most situations when considering donor kidneys, long cold-storage times are avoided. The identification of novel mechanisms of cold-storage-related renal damage will lead to the development of new therapeutic strategies for preserving donor kidneys; to date, these mechanisms remain poorly understood. In this review, we discuss the importance of mitochondrial function, protein homeostasis, and renal recovery during stress from cold storage plus transplantation. Additionally, we discuss novel targets for therapeutic intervention.
  • 1.2K
  • 09 Nov 2020
Topic Review
Ubiquitin-Like Proteins in Ribosome Production
Ubiquitin is a small protein that is highly conserved throughout eukaryotes. It operates as a reversible post-translational modifier through a process known as ubiquitination, which involves the addition of one or several ubiquitin moieties to a substrate protein. These modifications mark proteins for proteasome-dependent degradation or alter their localization or activity in a variety of cellular processes. In most eukaryotes, ubiquitin is generated by the proteolytic cleavage of precursor proteins in which it is fused either to itself, constituting a polyubiquitin precursor, or as a single N-terminal moiety to ribosomal proteins, which are practically invariably eL40 and eS31.
  • 540
  • 28 Apr 2021
Topic Review
Ubiquitin System
Ubiquitination of proteins is a post-translational modification process with many different cellular functions, including protein stability, immune signaling, antiviral functions and virus replication. While ubiquitination of viral proteins can be used by the host as a defense mechanism by destroying the incoming pathogen, viruses have adapted to take advantage of this cellular process. The ubiquitin system can be hijacked by viruses to enhance various steps of the replication cycle and increase pathogenesis. Emerging viruses, including severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), flaviviruses like Zika and dengue, as well as highly pathogenic viruses like Ebola and Nipah, have the ability to directly use the ubiquitination process to enhance their viral-replication cycle, and evade immune responses. Some of these mechanisms are conserved among different virus families, especially early during virus entry, providing an opportunity to develop broad-spectrum antivirals.
  • 714
  • 16 Jun 2021
Topic Review
Ubiquitin and Ubiquitin-like Proteins in T-Lymphocytes
Ubiquitination is a posttranslational modification that is involved in almost every cellular process. The most prominent function is the targeting of protein substrates for their degradation by the proteasome to maintain cellular protein homeostasis. Moreover, ubiquitination can serve many nonproteolytic functions like the regulation of protein kinase signaling, DNA damage response, intracellular trafficking, and transcription and translation. Ubiquitination is mediated by the transfer of the highly conserved 76 amino -acid protein ubiquitin to a target protein. Since T cells play a central role in the immune system and are indispensable for maintaining the adaptive cell mediated immunity, T cell signaling, and activation have to be tightly controlled. Like phosphorylation, ubiquitination is a reversible and highly dynamic process and critical for normal T cell function. In this regard, modification of T cell signaling proteins by ubiquitin or ubiquitin-related proteins is responsible not only for the initiation of T cell signaling but also for the termination of T cell activity.
  • 508
  • 15 Apr 2022
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