Next Article in Journal
Impact of Water Pollution on Trophic Transfer of Fatty Acids in Fish, Microalgae, and Zoobenthos in the Food Web of a Freshwater Ecosystem
Next Article in Special Issue
COP9 Signalosome Interaction with UspA/Usp15 Deubiquitinase Controls VeA-Mediated Fungal Multicellular Development
Previous Article in Journal
Maternal Leucine-Rich Diet Minimises Muscle Mass Loss in Tumour-bearing Adult Rat Offspring by Improving the Balance of Muscle Protein Synthesis and Degradation
Previous Article in Special Issue
Role of Cop9 Signalosome Subunits in the Environmental and Hormonal Balance of Plant
Open AccessFeature PaperEditor’s ChoiceReview

The Hunt for Degrons of the 26S Proteasome

Department of Biological Chemistry, Institute of Life Sciences, the Hebrew University of Jerusalem, Jerusalem 91904, Israel
*
Author to whom correspondence should be addressed.
Biomolecules 2019, 9(6), 230; https://doi.org/10.3390/biom9060230
Received: 28 May 2019 / Revised: 10 June 2019 / Accepted: 11 June 2019 / Published: 13 June 2019
(This article belongs to the Special Issue The Broader Cellular Impact of Proteasome-CSN-eIf3 (PCI) Complexes)
Since the discovery of ubiquitin conjugation as a cellular mechanism that triggers proteasomal degradation, the mode of substrate recognition by the ubiquitin-ligation system has been the holy grail of research in the field. This entails the discovery of recognition determinants within protein substrates, which are part of a degron, and explicit E3 ubiquitin (Ub)-protein ligases that trigger their degradation. Indeed, many protein substrates and their cognate E3′s have been discovered in the past 40 years. In the course of these studies, various degrons have been randomly identified, most of which are acquired through post-translational modification, typically, but not exclusively, protein phosphorylation. Nevertheless, acquired degrons cannot account for the vast diversity in cellular protein half-life times. Obviously, regulation of the proteome is largely determined by inherent degrons, that is, determinants integral to the protein structure. Inherent degrons are difficult to predict since they consist of diverse sequence and secondary structure features. Therefore, unbiased methods have been employed for their discovery. This review describes the history of degron discovery methods, including the development of high throughput screening methods, state of the art data acquisition and data analysis. Additionally, it summarizes major discoveries that led to the identification of cognate E3 ligases and hitherto unrecognized complexities of degron function. Finally, we discuss future perspectives and what still needs to be accomplished towards achieving the goal of understanding how the eukaryotic proteome is regulated via coordinated action of components of the ubiquitin-proteasome system. View Full-Text
Keywords: ubiquitin-proteasome system; degrons; E3-ubiquitin ligases; protein quality control; high throughput screens; next generation sequencing ubiquitin-proteasome system; degrons; E3-ubiquitin ligases; protein quality control; high throughput screens; next generation sequencing
Show Figures

Figure 1

MDPI and ACS Style

Ella, H.; Reiss, Y.; Ravid, T. The Hunt for Degrons of the 26S Proteasome. Biomolecules 2019, 9, 230. https://doi.org/10.3390/biom9060230

AMA Style

Ella H, Reiss Y, Ravid T. The Hunt for Degrons of the 26S Proteasome. Biomolecules. 2019; 9(6):230. https://doi.org/10.3390/biom9060230

Chicago/Turabian Style

Ella, Hadar; Reiss, Yuval; Ravid, Tommer. 2019. "The Hunt for Degrons of the 26S Proteasome" Biomolecules 9, no. 6: 230. https://doi.org/10.3390/biom9060230

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop