Modification of glyceraldehyde-3-phosphate dehydrogenase with nitric oxide: role in signal transduction and development of apoptosis

Muronetz, V.I.; Medvedeva, M.V.; Sevostyanova, I.A.; Schmalhausen, E.V.

Авторы: Muronetz V.I., Medvedeva M.V., Sevostyanova I.A., Schmalhausen E.V.
Журнал: Biomolecules
Том: 11
Номер: 11
Год издания: 2021
Издательство: MDPI
Местоположение издательства: Basel, Switzerland
Первая страница: 1656
DOI: 10.3390/biom11111656
Аннотация: The review focuses on the consequences of GAPDH S-nitrosylation at the catalytic cysteine residue. The widespread hypothesis according to which S-nitrosylation causes a change in GAPDH structure and its subsequent binding to Siah1 protein is considered in most detail. It is assumed that the GAPDH complex with Siah1 is transported to the nucleus due to 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 S-nitrosylation of GAPDH. The question remains whether the translocation of GAPDH into the nucleus is caused by S-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+ 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 solution of which will make it possible more definitely establish the role of nitric oxide in the induction of apoptosis.
Добавил в систему: Медведева Мария Витальевна

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Modification of glyceraldehyde-3-phosphate dehydrogenase with nitric oxide: role in signal transduction and development of apoptosisстатья

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