Next Article in Journal
Cerrena unicolor Laccases, Genes Expression and Regulation of Activity
Next Article in Special Issue
Saccharomyces cerevisiae as a Toolkit for COP9 Signalosome Research
Previous Article in Journal
Chemoinformatic Screening for the Selection of Potential Senolytic Compounds from Natural Products
Previous Article in Special Issue
Urm1: A Non-Canonical UBL
Open AccessReview

The Cys Sense: Thiol Redox Switches Mediate Life Cycles of Cellular Proteins

1
Department of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, Safra Campus Givat Ram, The Hebrew University of Jerusalem, Jerusalem 91904, Israel
2
Institute of Chemistry, Safra Campus Givat Ram, The Hebrew University of Jerusalem, Jerusalem 91904, Israel
*
Author to whom correspondence should be addressed.
Academic Editors: Sonia Longhi and Elah Pick
Biomolecules 2021, 11(3), 469; https://doi.org/10.3390/biom11030469
Received: 19 December 2020 / Revised: 15 March 2021 / Accepted: 16 March 2021 / Published: 22 March 2021
(This article belongs to the Special Issue Ubiquitin-Like Modifiers and Their Diverse Impact on Cell Signaling)
Protein homeostasis is an essential component of proper cellular function; however, sustaining protein health is a challenging task, especially during the aerobic lifestyle. Natural cellular oxidants may be involved in cell signaling and antibacterial defense; however, imbalanced levels can lead to protein misfolding, cell damage, and death. This merges together the processes of protein homeostasis and redox regulation. At the heart of this process are redox-regulated proteins or thiol-based switches, which carefully mediate various steps of protein homeostasis across folding, localization, quality control, and degradation pathways. In this review, we discuss the “redox code” of the proteostasis network, which shapes protein health during cell growth and aging. We describe the sources and types of thiol modifications and elaborate on diverse strategies of evolving antioxidant proteins in proteostasis networks during oxidative stress conditions. We also highlight the involvement of cysteines in protein degradation across varying levels, showcasing the importance of cysteine thiols in proteostasis at large. The individual examples and mechanisms raised open the door for extensive future research exploring the interplay between the redox and protein homeostasis systems. Understanding this interplay will enable us to re-write the redox code of cells and use it for biotechnological and therapeutic purposes. View Full-Text
Keywords: thiol switches; proteostasis; chaperones; protein degradation; oxidative stress; redox-regulated proteins thiol switches; proteostasis; chaperones; protein degradation; oxidative stress; redox-regulated proteins
Show Figures

Figure 1

MDPI and ACS Style

Radzinski, M.; Oppenheim, T.; Metanis, N.; Reichmann, D. The Cys Sense: Thiol Redox Switches Mediate Life Cycles of Cellular Proteins. Biomolecules 2021, 11, 469. https://doi.org/10.3390/biom11030469

AMA Style

Radzinski M, Oppenheim T, Metanis N, Reichmann D. The Cys Sense: Thiol Redox Switches Mediate Life Cycles of Cellular Proteins. Biomolecules. 2021; 11(3):469. https://doi.org/10.3390/biom11030469

Chicago/Turabian Style

Radzinski, Meytal; Oppenheim, Tal; Metanis, Norman; Reichmann, Dana. 2021. "The Cys Sense: Thiol Redox Switches Mediate Life Cycles of Cellular Proteins" Biomolecules 11, no. 3: 469. https://doi.org/10.3390/biom11030469

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