Adp-Ribosylation

Ueda, Kunihiro; Hayaishi, Osamu

doi:10.1146/annurev.bi.54.070185.000445

Cited by 747 publications

(257 citation statements)

References 0 publications

Supporting

Mentioning

255

Contrasting

Order By: Relevance

“…Many GTP-binding proteins, including transducin and the regulatory subunits of adenylate cyclase, possess similarities in structure and are ADP-ribosylated by microbial toxins. Most substrates are also GTPases [14]. We have shown that a highly conserved non-ribosomal 22 kDa protein exists in membranes derived from the ER of protein-secreting tissues and is ADPribosylated by cholera toxin under conditions similar to those described for the adenylate cyclase stimulatory subunit Gs [15] in that labelling is enhanced by GTP.…”

Section: Discussionmentioning

confidence: 99%

“…la, track 9). In the presence of GTP, labelling of the 22 kDa protein was slightly enhanced by increasing substrate concentration of NAD + up to 10/zM (tracks 10-12), whereas at higher concentrations of NAD ÷ the label was diluted out (tracks 13,14). The Coomassie bluestained profiles corresponding to tracks 4 and 5 are shown in tracks 2 and 3.…”

Section: Proteins In Canine Pancreatic Stripped Microsomes [32p]adp-rmentioning

confidence: 99%

See 1 more Smart Citation

GTP‐dependent ADP‐ribosylation of a 22 kDa protein in the endoplasmic reticulum membrane

Robinson

Austen

1987

FEBS Letters

View full text Add to dashboard Cite

Treatment of salt-stripped rough microsomal membranes from pancreas or liver with NAD and cholera toxin in the presence of GTP yields an ADP-ribosylated non-ribosomal 22 kDa protein. Membranes containing the modified protein are less active in the co-translational processing of secretory preproteins translated from isolated mRNA in a reticuloeyte translation system, but signal peptidase activity is unchanged, suggesting that the 22 kDa protein is involved in the targetting or translocation of secretory proteins at the membrane of the endoplasmic reticulum.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Proteins In Canine Pancreatic Stripped Microsomes [32p]adp-rmentioning

confidence: 99%

GTP‐dependent ADP‐ribosylation of a 22 kDa protein in the endoplasmic reticulum membrane

Robinson

Austen

1987

FEBS Letters

View full text Add to dashboard Cite

show abstract

“…As has also been reported for cholera and pertussis toxin [l, 191, rather high concentrations of nicotinamide (100 mM) were necessary for a blockade of the ADP-ribosylation by botulinum toxin. ADP-ribosylation of proteins is typically sensitive to snake venom phosphodiesterase [20]. Treatment of the ADP-ribosylated 43-kDa substrate protein with Crotaulus phosphodiesterase (0.02 U) for 1 h completely cleaved the radiolabel (not shown).…”

Section: Adp-ribosylation Of Actin In Platelet Cytosolmentioning

confidence: 98%

ADP‐ribosylation of platelet actin by botulinum C2 toxin

Aktories¹,

Ankenbauer

Schering³

et al. 1986

European Journal of Biochemistry

View full text Add to dashboard Cite

Botulinum C2 toxin is a microbial toxin which possesses ADP-ribosyltransferase activity. In human platelet cytosol a 43-kDa protein was ADP-ribosylated by botulinum C2 toxin. Labelling of the 43-kDa protein using [32P]NAD as substrate was reduced by unlabelled NAD and nicotinamide. The label was removed by treatment with snake venom phosphodiesterase. Half-maximal and maximal ADP-ribosylation occurred at 0.1 pg/ml and 3 pg/ml botulinum C2 toxin, respectively. The K , value of the ADP-ribosylation reaction for NAD was about 1 pM. The peptide map of the ADP-ribosylated 43-kDa protein was almost identical with platelet actin. The ADP-ribosylated 43-kDa substrate protein bound to and was eluted from immobilized DNase I in a manner similar to G-actin. Trypsin treatment of platelet cytosol decreased subsequent ADP-ribosylation of the 43-kDa protein without occurrence of smaller labelled polypeptides. Purified platelet actin was also ADP-ribosylated by botulinum C2 toxin with similar characteristics found with actin in platelet cytosol. Phalloidin decreased the ADP-ribosylation of actin in platelet cytosol and of isolated platelet actin. Half-maximal and maximal, about 90%, reduction of actin ADP-ribosylation was observed at 0.4 pM and 10 pM phalloidin, respectively. ADPribosylation of purified actin, induced by botulinum C21 toxin, abolished the formation of the typical microfilament network. The data indicate that platelet G-actin but not F-actin is a substrate of botulinum C2 toxin and that this covalent modification largely affects the functional properties of actin.

show abstract

“…Mono-ADP-ribosylation is a post-translational modification of proteins whereby the adenosine 5Ј-diphosphoribose moiety of NAD ϩ is transferred to one of a number of amino acid residues (1,2). Several well characterized mono-ADP-ribosylation reactions are catalyzed by bacterial toxins and result in the permanent modification of GTPases with key regulatory functions in cellular processes (1,2).…”

mentioning

confidence: 99%

“…Several well characterized mono-ADP-ribosylation reactions are catalyzed by bacterial toxins and result in the permanent modification of GTPases with key regulatory functions in cellular processes (1,2). Similar reactions are also catalyzed by eukaryotic enzymes, but their cellular significance, despite recent advances (3)(4)(5), is less well understood.…”

mentioning

confidence: 99%

Characterization of Chemical Inhibitors of Brefeldin A-activated Mono-ADP-ribosylation

Weigert

Colanzi

Mirоnоv

et al. 1997

Journal of Biological Chemistry

View full text Add to dashboard Cite

Brefeldin A, a toxin inhibitor of vesicular traffic, induces the selective mono-ADP-ribosylation of two cytosolic proteins, glyceraldehyde-3-phosphate dehydrogenase and the novel GTP-binding protein BARS-50. Here, we have used a new quantitative assay for the characterization of this reaction and the development of specific pharmacological inhibitors. Mono-ADP-ribosylation is activated by brefeldin A with an EC 50 of 17.0 ؎ 3.1 g/ml, but not by biologically inactive analogs including a brefeldin A stereoisomer. Brefeldin A acts by increasing the V max of the reaction, whereas it does not influence the K m of the enzyme for NAD ؉ (154 ؎ 13 M). The enzyme is an integral membrane protein present in most tissues and is modulated by Zn 2؉ , Cu 2؉ , ATP (but not by other nucleotides), pH, temperature, and ionic strength. To identify inhibitors of the reaction, a large number of drugs previously tested as blockers of bacterial ADPribosyltransferases were screened. Two classes of molecules, one belonging to the coumarin group (dicumarol, coumermycin A 1 , and novobiocin) and the other to the quinone group (ilimaquinone, benzoquinone, and naphthoquinone), rather potently and specifically inhibited brefeldin A-dependent mono-ADP-ribosylation. When tested in living cells, these molecules antagonized the tubular reticular redistribution of the Golgi complex caused by brefeldin A at concentrations similar to those active in the mono-ADP-ribosylation assay in vitro, suggesting a role for mono-ADP-ribosylation in the cellular actions of brefeldin A.Mono-ADP-ribosylation is a post-translational modification of proteins whereby the adenosine 5Ј-diphosphoribose moiety of NAD ϩ is transferred to one of a number of amino acid residues (1, 2). Several well characterized mono-ADP-ribosylation reactions are catalyzed by bacterial toxins and result in the permanent modification of GTPases with key regulatory functions in cellular processes (1, 2). Similar reactions are also catalyzed by eukaryotic enzymes, but their cellular significance, despite recent advances (3-5), is less well understood. Recently, we have reported that brefeldin A (BFA), 1 a fungal toxin metabolite of palmitic acid (6) with potent inhibitory effects on intracellular membrane traffic (7), stimulates the selective mono-ADP-ribosylation of two cytosolic proteins of 38 and 50 kDa in mammalian cells (8). The 50-kDa substrate (BARS-50; see Ref. 9) binds GTP and is regulated by ␤␥-subunits of trimeric G proteins; it has therefore been proposed to be a novel G protein involved in membrane transport (9). The p38 substrate is glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a multifunctional protein involved in several cellular processes (10 -16). These observations have raised the question as to whether some of the cellular effects of BFA might be mediated by mono-ADP-ribosylation.The cellular actions of BFA are multiple and complex. BFA selectively blocks constitutive protein secretion and causes a rapid and extensive disruption of the Golgi apparatus consisting of the ...

show abstract

Adp-Ribosylation

Cited by 747 publications

References 0 publications

GTP‐dependent ADP‐ribosylation of a 22 kDa protein in the endoplasmic reticulum membrane

GTP‐dependent ADP‐ribosylation of a 22 kDa protein in the endoplasmic reticulum membrane

ADP‐ribosylation of platelet actin by botulinum C2 toxin

Characterization of Chemical Inhibitors of Brefeldin A-activated Mono-ADP-ribosylation

Contact Info

Product

Resources

About