Glyceraldehyde‐3‐phosphate activates auto‐ADP‐ribosylation of glyceraldehyde‐3‐phosphate dehydrogenase

Kots, Alexander Y.; Sergienko, Edward A.; Bulargina, T. V.; Severin, E. S.

doi:10.1016/0014-5793(93)81526-6

Cited by 11 publications

(5 citation statements)

References 20 publications

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“…While the distribution of ARTs and ARHs in nucleus and cytoplasm has been quite well described, the existence and distribution of ADP-ribosylating enzymes in mitochondria remains thus controversial. Five enzymes able to regulate ADP-ribosylation have so far been associated with mitochondria: SIRT4 [94,127], ARTD1, PARG, ARH3 [92,128], and MacroD1 [93,129]. ART activity has, in fact, been detected in the mitochondrial matrix, as well as the inner- and outer mitochondrial membranes [130].…”

Section: Mitochondrial Nad Biosynthesis Adp-ribosylation Crosstalmentioning

confidence: 99%

“…MacroD1: MacroD1 has been shown to be active towards mono-ADP-ribosylated proteins, as well as toward free OAADPR, the by-product of SIRT-catalyzed de-acetylation [88,89,129]. In contrast to the four enzymes discussed above, MacroD1 has been clearly shown to predominantly localize to mitochondria [93,129]. Available transcriptome data from humans, mice, and rats [149] suggest that MacroD1 expression correlates with the energetic status of a given cell or tissue type.…”

Section: Mitochondrial Nad Biosynthesis Adp-ribosylation Crosstalmentioning

confidence: 99%

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Regulation of Glucose Metabolism by NAD+ and ADP-Ribosylation

Hopp

Grüter

Hottiger

2019

Cells

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Cells constantly adapt their metabolic pathways to meet their energy needs and respond to nutrient availability. During the last two decades, it has become increasingly clear that NAD+, a coenzyme in redox reactions, also mediates several ubiquitous cell signaling processes. Protein ADP-ribosylation is a post-translational modification that uses NAD+ as a substrate and is best known as part of the genotoxic stress response. However, there is increasing evidence that NAD+-dependent ADP-ribosylation regulates other cellular processes, including metabolic pathways. In this review, we will describe the compartmentalized regulation of NAD+ biosynthesis, consumption, and regeneration with a particular focus on the role of ADP-ribosylation in the regulation of glucose metabolism in different cellular compartments.

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Section: Mitochondrial Nad Biosynthesis Adp-ribosylation Crosstalmentioning

confidence: 99%

Section: Mitochondrial Nad Biosynthesis Adp-ribosylation Crosstalmentioning

confidence: 99%

Regulation of Glucose Metabolism by NAD+ and ADP-Ribosylation

Hopp

Grüter

Hottiger

2019

Cells

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“…The level of understanding of the nature of these endogenous ADP-ribosyltransferases is poor relative to the extent ofknowledge concerning the bacterial toxins. Not all of the target proteins have been identified, and it is not clear whether all of the modifications reported require an ADP-ribosyltransferase to catalyse the reaction, or if they may proceed non-enzymically [12][13][14]. Some target proteins, such as G,a and G,a, are modified by both endogenous enzymes and bacterial toxins.…”

Section: Introductionmentioning

confidence: 99%

The purification of a cysteine-dependent NAD+ glycohydrolase activity from bovine erythrocytes and evidence that it exhibits a novel ADP-ribosyltransferase activity

Saxty

Heyningen

1995

Biochemical Journal

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An NAD+:cysteine ADP-ribosyltransferase activity was purified from bovine erythrocytes on the assumption that, like pertussis toxin, the enzyme would exhibit a cysteine-dependent NAD+ glycohydrolase activity. A three-step purification procedure was developed involving (1) precipitation with 40% (NH4)2SO4, (2) binding to a cysteine-Sepharose affinity column, and (3) binding to an NAD+ affinity column. PAGE showed a single band of M(r) 45,000. The enzyme had been purified 47,000-fold and had a specific activity of 1900 nmol nicotinamide released/min per mg. A study of the kinetic properties of this enzyme showed saturation kinetics for cysteine (Km = 4.0 mM). The ability of this enzyme to ADP-ribosylate protein was investigated using re-sealed inverted bovine erythrocyte ghosts. Incubation of the purified enzyme with erythrocyte ghosts and [adenylate-32P]NAD+ led to the enhanced dose-dependent labelling of several proteins, a doublet of high M(r) and proteins of M(r) 60,000, 55,000 and 29,000, identified by autoradiography of separated proteins on SDS/PAGE. The enzyme-catalysed labelling of the major component at M(r) 55,000 was blocked by pre-treatment of the erythrocyte ghosts with N-ethymaleimide, a sulphydryl alkylating agent, and the label was released by mercuric ion, but not by hydroxylamine. These experiments suggested that a cysteine residue on the target protein had been mono-ADP-ribosylated. This supposition was further supported by identification of the mercf1p4ion-released radiolabelled product as ADP-ribose by HPLC, and the observation that free ADP-ribose was unable to modify the membrane target protein directly.

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“…Secreted GAPDH from Entamoeba histolytica was also found to be ADP-ribosylated [16]. The auto-catalysis of ADP-ribosylation of GAPDH is enhanced by the substrate, D-glyceraldehyde 3-phosphate [17]. Others have shown that nitric oxide promotes ADP-ribosylation [18].…”

Section: Auto-catalytic Processesmentioning

confidence: 90%

Target for Diverse Chemical Modifications

Seidler

2012

GAPDH: Biological Properties and Diversity

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The chapter begins with an historical perspective of GAPDH isozymes that is juxtaposed to the fact that there is only one somatic functional gene in humans that is virtually identical among the mammalian species. Over the many years of GAPDH research, dozens of labs have reported the existence of multiple forms of GAPDH, which mostly vary as a function of charge with an occasional report of truncated forms. These observations are in part due to GAPDH being a substrate for many enzymatically-controlled post-translational modifications. While target residues have been identified and predictive algorithms have implicated certain residues, this area of research appears to be in its infancy regarding GAPDH. Equally fascinating, the uniquely susceptible nature of GAPDH to non-enzymatic reactions, that typically are associated with cell stress, such as oxidation and nitration, is also discussed. Two metabolic gases, nitric oxide and hydrogen sulfide, which are enzymatically produced, appear to exert their signaling properties through non-enzymatic reaction with GAPDH. Models of cellular decline are also proposed, including the compelling hypothesis that states cell compromise occurs by the physically blocking the function of chaperonins (i.e. dual-ring multiple-subunit molecular chaperones) by the attachment of misfolded GAPDH.

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Glyceraldehyde‐3‐phosphate activates auto‐ADP‐ribosylation of glyceraldehyde‐3‐phosphate dehydrogenase

Cited by 11 publications

References 20 publications

Regulation of Glucose Metabolism by NAD+ and ADP-Ribosylation

Regulation of Glucose Metabolism by NAD+ and ADP-Ribosylation

The purification of a cysteine-dependent NAD+ glycohydrolase activity from bovine erythrocytes and evidence that it exhibits a novel ADP-ribosyltransferase activity

Target for Diverse Chemical Modifications

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