Modification of Glyceraldehyde-3-Phosphate Dehydrogenase with Nitric Oxide: Role in Signal Transduction and Development of Apoptosis

This review focuses on the consequences of GAPDH <i>S</i>-nitrosylation at the catalytic cysteine residue. The widespread hypothesis according to which <i>S</i>-nitrosylation causes a change in GAPDH structure and its subsequent binding to the Siah1 protein is considered in d...

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Autores principales:	Vladimir I. Muronetz, Maria V. Medvedeva, Irina A. Sevostyanova, Elena V. Schmalhausen
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	glyceraldehyde-3-phosphate dehydrogenase <i>S</i>-nitrosylation protein–protein interactions oxidation sulfenic acid NO Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/e0d37a8968e44f25839b2c93f5ab8840
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spelling	oai:doaj.org-article:e0d37a8968e44f25839b2c93f5ab88402021-11-25T16:53:25ZModification of Glyceraldehyde-3-Phosphate Dehydrogenase with Nitric Oxide: Role in Signal Transduction and Development of Apoptosis10.3390/biom111116562218-273Xhttps://doaj.org/article/e0d37a8968e44f25839b2c93f5ab88402021-11-01T00:00:00Zhttps://www.mdpi.com/2218-273X/11/11/1656https://doaj.org/toc/2218-273XThis review focuses on the consequences of GAPDH <i>S</i>-nitrosylation at the catalytic cysteine residue. The widespread hypothesis according to which <i>S</i>-nitrosylation causes a change in GAPDH structure and its subsequent binding to the Siah1 protein is considered in detail. It is assumed that the GAPDH complex with Siah1 is transported to the nucleus by carrier proteins, interacts with nuclear proteins, and induces apoptosis. However, there are several conflicting and unproven elements in this hypothesis. In particular, there is no direct confirmation of the interaction between the tetrameric GAPDH and Siah1 caused by <i>S</i>-nitrosylation of GAPDH. The question remains as to whether the translocation of GAPDH into the nucleus is caused by <i>S</i>-nitrosylation or by some other modification of the catalytic cysteine residue. The hypothesis of the induction of apoptosis by oxidation of GAPDH is considered. This oxidation leads to a release of the coenzyme NAD<sup>+</sup> from the active center of GAPDH, followed by the dissociation of the tetramer into subunits, which move to the nucleus due to passive transport and induce apoptosis. In conclusion, the main tasks are summarized, the solutions to which will make it possible to more definitively establish the role of nitric oxide in the induction of apoptosis.Vladimir I. MuronetzMaria V. MedvedevaIrina A. SevostyanovaElena V. SchmalhausenMDPI AGarticleglyceraldehyde-3-phosphate dehydrogenase<i>S</i>-nitrosylationprotein–protein interactionsoxidationsulfenic acidNOMicrobiologyQR1-502ENBiomolecules, Vol 11, Iss 1656, p 1656 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	glyceraldehyde-3-phosphate dehydrogenase <i>S</i>-nitrosylation protein–protein interactions oxidation sulfenic acid NO Microbiology QR1-502
spellingShingle	glyceraldehyde-3-phosphate dehydrogenase <i>S</i>-nitrosylation protein–protein interactions oxidation sulfenic acid NO Microbiology QR1-502 Vladimir I. Muronetz Maria V. Medvedeva Irina A. Sevostyanova Elena V. Schmalhausen Modification of Glyceraldehyde-3-Phosphate Dehydrogenase with Nitric Oxide: Role in Signal Transduction and Development of Apoptosis
description	This review focuses on the consequences of GAPDH <i>S</i>-nitrosylation at the catalytic cysteine residue. The widespread hypothesis according to which <i>S</i>-nitrosylation causes a change in GAPDH structure and its subsequent binding to the Siah1 protein is considered in detail. It is assumed that the GAPDH complex with Siah1 is transported to the nucleus by carrier proteins, interacts with nuclear proteins, and induces apoptosis. However, there are several conflicting and unproven elements in this hypothesis. In particular, there is no direct confirmation of the interaction between the tetrameric GAPDH and Siah1 caused by <i>S</i>-nitrosylation of GAPDH. The question remains as to whether the translocation of GAPDH into the nucleus is caused by <i>S</i>-nitrosylation or by some other modification of the catalytic cysteine residue. The hypothesis of the induction of apoptosis by oxidation of GAPDH is considered. This oxidation leads to a release of the coenzyme NAD<sup>+</sup> from the active center of GAPDH, followed by the dissociation of the tetramer into subunits, which move to the nucleus due to passive transport and induce apoptosis. In conclusion, the main tasks are summarized, the solutions to which will make it possible to more definitively establish the role of nitric oxide in the induction of apoptosis.
format	article
author	Vladimir I. Muronetz Maria V. Medvedeva Irina A. Sevostyanova Elena V. Schmalhausen
author_facet	Vladimir I. Muronetz Maria V. Medvedeva Irina A. Sevostyanova Elena V. Schmalhausen
author_sort	Vladimir I. Muronetz
title	Modification of Glyceraldehyde-3-Phosphate Dehydrogenase with Nitric Oxide: Role in Signal Transduction and Development of Apoptosis
title_short	Modification of Glyceraldehyde-3-Phosphate Dehydrogenase with Nitric Oxide: Role in Signal Transduction and Development of Apoptosis
title_full	Modification of Glyceraldehyde-3-Phosphate Dehydrogenase with Nitric Oxide: Role in Signal Transduction and Development of Apoptosis
title_fullStr	Modification of Glyceraldehyde-3-Phosphate Dehydrogenase with Nitric Oxide: Role in Signal Transduction and Development of Apoptosis
title_full_unstemmed	Modification of Glyceraldehyde-3-Phosphate Dehydrogenase with Nitric Oxide: Role in Signal Transduction and Development of Apoptosis
title_sort	modification of glyceraldehyde-3-phosphate dehydrogenase with nitric oxide: role in signal transduction and development of apoptosis
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/e0d37a8968e44f25839b2c93f5ab8840
work_keys_str_mv	AT vladimirimuronetz modificationofglyceraldehyde3phosphatedehydrogenasewithnitricoxideroleinsignaltransductionanddevelopmentofapoptosis AT mariavmedvedeva modificationofglyceraldehyde3phosphatedehydrogenasewithnitricoxideroleinsignaltransductionanddevelopmentofapoptosis AT irinaasevostyanova modificationofglyceraldehyde3phosphatedehydrogenasewithnitricoxideroleinsignaltransductionanddevelopmentofapoptosis AT elenavschmalhausen modificationofglyceraldehyde3phosphatedehydrogenasewithnitricoxideroleinsignaltransductionanddevelopmentofapoptosis
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Modification of Glyceraldehyde-3-Phosphate Dehydrogenase with Nitric Oxide: Role in Signal Transduction and Development of Apoptosis

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