The Cys Sense: Thiol Redox Switches Mediate Life Cycles of Cellular Proteins
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...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-03-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/11/3/469 |
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| author | Meytal Radzinski Tal Oppenheim Norman Metanis Dana Reichmann |
| author_facet | Meytal Radzinski Tal Oppenheim Norman Metanis Dana Reichmann |
| author_sort | Meytal Radzinski |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T13:00:56Z |
| format | Article |
| id | doaj.art-62b2261475a14147bc79a27b89e54089 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-10T13:00:56Z |
| publishDate | 2021-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-62b2261475a14147bc79a27b89e540892023-11-21T11:29:02ZengMDPI AGBiomolecules2218-273X2021-03-0111346910.3390/biom11030469The Cys Sense: Thiol Redox Switches Mediate Life Cycles of Cellular ProteinsMeytal Radzinski0Tal Oppenheim1Norman Metanis2Dana Reichmann3Department of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, Safra Campus Givat Ram, The Hebrew University of Jerusalem, Jerusalem 91904, IsraelDepartment of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, Safra Campus Givat Ram, The Hebrew University of Jerusalem, Jerusalem 91904, IsraelInstitute of Chemistry, Safra Campus Givat Ram, The Hebrew University of Jerusalem, Jerusalem 91904, IsraelDepartment of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, Safra Campus Givat Ram, The Hebrew University of Jerusalem, Jerusalem 91904, IsraelProtein 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.https://www.mdpi.com/2218-273X/11/3/469thiol switchesproteostasischaperonesprotein degradationoxidative stressredox-regulated proteins |
| spellingShingle | Meytal Radzinski Tal Oppenheim Norman Metanis Dana Reichmann The Cys Sense: Thiol Redox Switches Mediate Life Cycles of Cellular Proteins Biomolecules thiol switches proteostasis chaperones protein degradation oxidative stress redox-regulated proteins |
| title | The Cys Sense: Thiol Redox Switches Mediate Life Cycles of Cellular Proteins |
| title_full | The Cys Sense: Thiol Redox Switches Mediate Life Cycles of Cellular Proteins |
| title_fullStr | The Cys Sense: Thiol Redox Switches Mediate Life Cycles of Cellular Proteins |
| title_full_unstemmed | The Cys Sense: Thiol Redox Switches Mediate Life Cycles of Cellular Proteins |
| title_short | The Cys Sense: Thiol Redox Switches Mediate Life Cycles of Cellular Proteins |
| title_sort | cys sense thiol redox switches mediate life cycles of cellular proteins |
| topic | thiol switches proteostasis chaperones protein degradation oxidative stress redox-regulated proteins |
| url | https://www.mdpi.com/2218-273X/11/3/469 |
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