Version 1
: Received: 30 November 2020 / Approved: 1 December 2020 / Online: 1 December 2020 (13:14:47 CET)
How to cite:
Tossounian, M.; Zhang, B.; Gout, I. The Writers, Readers and Erasers in Redox Regulation of GAPDH. Preprints2020, 2020120024. https://doi.org/10.20944/preprints202012.0024.v1
Tossounian, M.; Zhang, B.; Gout, I. The Writers, Readers and Erasers in Redox Regulation of GAPDH. Preprints 2020, 2020120024. https://doi.org/10.20944/preprints202012.0024.v1
Tossounian, M.; Zhang, B.; Gout, I. The Writers, Readers and Erasers in Redox Regulation of GAPDH. Preprints2020, 2020120024. https://doi.org/10.20944/preprints202012.0024.v1
APA Style
Tossounian, M., Zhang, B., & Gout, I. (2020). The Writers, Readers and Erasers in Redox Regulation of GAPDH. Preprints. https://doi.org/10.20944/preprints202012.0024.v1
Chicago/Turabian Style
Tossounian, M., Bruce Zhang and Ivan Gout. 2020 "The Writers, Readers and Erasers in Redox Regulation of GAPDH" Preprints. https://doi.org/10.20944/preprints202012.0024.v1
Abstract
Glyceraldehyde 3–phosphate dehydrogenase (GAPDH) is a key glycolytic enzyme, which is crucial for the breakdown of glucose to provide cellular energy. Over the past decade, GAPDH has been reported to be one of the most prominent cellular targets of post-translational modifications (PTMs), which divert GAPDH towards different non-glycolytic functions. Hence, it is termed a moonlighting protein. During metabolic and oxidative stress, GAPDH is a target of different oxidative PTMs (oxPTM), e.g. sulfenylation, S-thiolation, nitrosylation and sulfhydration. These modifications alter the enzyme’s conformation, subcellular localization and regulatory interactions with downstream partners, which impact its glycolytic and non-glycolytic functions. In this review, we discuss the redox regulation of GAPDH by different redox writers, which introduce the oxPTM code on GAPDH to instruct a redox response; the GAPDH readers, which decipher the oxPTM code through regulatory interactions and coordinate cellular response via the formation of multi-enzyme signaling complexes; and the redox erasers, which are the reducing systems that regenerate the GAPDH catalytic activity. Human pathologies associated with the oxidation-induced dysregulation of GAPDH are also discussed, featuring the importance of the redox regulation of GAPDH in neurodegeneration and metabolic disorders.
Biology and Life Sciences, Biochemistry and Molecular Biology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
