Binding of glyceraldehyde-3-phosphate dehydrogenase to G-actin promotes the transnitrosylation reaction.

Autor: Medvedeva MV; Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119991, Russia., Serebryakova MV; Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119991, Russia., Matyushenko AM; Bach Institute of Biochemistry, Research Center of Biotechnology, Russian Academy of Sciences, Moscow, 119071, Russia., Nefedova VV; Bach Institute of Biochemistry, Research Center of Biotechnology, Russian Academy of Sciences, Moscow, 119071, Russia., Muronetz VI; Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119991, Russia; Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, 119991, Russia., Schmalhausen EV; Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119991, Russia. Electronic address: shmal@belozersky.msu.ru.
Jazyk: angličtina
Zdroj: Archives of biochemistry and biophysics [Arch Biochem Biophys] 2024 Dec; Vol. 762, pp. 110189. Date of Electronic Publication: 2024 Oct 29.
DOI: 10.1016/j.abb.2024.110189
Abstrakt: In this study, we investigated formation of the complex between glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and actin and the possibility of nitrosyl group transfer between GAPDH and actin. A complex of GAPDH with beta-actin was isolated from lysates of HEK293T cells using immunoprecipitation with antibodies against GAPDH or against beta-actin. The treatment of the cells with H 2 O 2 or NO donor did not affect the formation of the complex. Investigation of the interaction between purified GAPDH and muscle alpha-actin showed that GAPDH interacts better with globular (G-) actin than with fibrillary actin, and oxidation/reduction of GAPDH does not affect this interaction. S-nitrosylated GAPDH (GAPDH-SNO) was partially reactivated in the presence of G-actin, which was accompanied by denitrosylation of GAPDH and sulfenation of G-actin. The sulfenated cysteine residue in G-actin was identified by MALDI-TOF MS analysis as C-terminal Cys374. Based on the properties of nitrosothiols, we assume that the cysteine-sulfenic acid in actin is a product of spontaneous hydrolysis of S-nitrosylated cysteine residue. The obtained results suggest that Cys374 in actin is S-nitrosylated during the incubation with GAPDH-SNO (transnitrosylation reaction). The transfer of the NO-group from GAPDH-SNO to the C-terminal Cys374 of actin suggests that upon interaction with GAPDH, the C-terminus of actin is located in the active center of GAPDH in the proximity to the catalytic Cys152. It is possible that the ability of GAPDH-SNO to nitrosylate actin contributes to the redox regulation of actin-controlled signaling pathways.
Competing Interests: Declaration of competing interest The authors declare no conflicts of interest.
(Copyright © 2024 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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