Mechanism of Cholera Toxin Action: ADP-Ribosylation Factors as Stimulators of Cholera Toxin-Catalyzed ADP-Ribosylation and Effectors in Intracellular Vesicular Trafficking Events

A second guanyl nucleotide-binding site associated with adenylate cyclase. Distinct nucleotides activate adenylate cyclase and permit ADP-ribosylation by cholera toxin.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)44319-5 ◽

1983 ◽

Vol 258 (19) ◽

pp. 11908-11914 ◽

Cited By ~ 4

Author(s):

D M Gill ◽

R Meren

Keyword(s):

Adenylate Cyclase ◽

Binding Site ◽

Cholera Toxin ◽

Nucleotide Binding ◽

Nucleotide Binding Site ◽

Adp Ribosylation

Characterization of the human gene encoding ADP-ribosylation factor 1, a guanine nucleotide-binding activator of cholera toxin.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)50383-0 ◽

1992 ◽

Vol 267 (13) ◽

pp. 9028-9034

Author(s):

C.M. Lee ◽

R.S. Haun ◽

S.C. Tsai ◽

J Moss ◽

M Vaughan

Keyword(s):

Cholera Toxin ◽

Human Gene ◽

Nucleotide Binding ◽

Guanine Nucleotide ◽

Gene Encoding ◽

Adp Ribosylation ◽

Guanine Nucleotide Binding ◽

Adp Ribosylation Factor

Requirements for cholera toxin-dependent ADP-ribosylation of the purified regulatory component of adenylate cyclase.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)68316-x ◽

1982 ◽

Vol 257 (1) ◽

pp. 20-23 ◽

Cited By ~ 6

Author(s):

L.S. Schleifer ◽

R.A. Kahn ◽

E. Hanski ◽

J.K. Northup ◽

P.C. Sternweis ◽

...

Keyword(s):

Adenylate Cyclase ◽

Cholera Toxin ◽

Adp Ribosylation

Chemotactic Peptide Receptor-supported ADP-Ribosylation of a Pertussis Toxin Substrate GTP-binding Protein by Cholera Toxin in Neutrophil-type HL-60 Cells

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)30093-6 ◽

1989 ◽

Vol 264 (35) ◽

pp. 21394-21400

Author(s):

T Iiri ◽

M Tohkin ◽

N Morishima ◽

Y Ohoka ◽

M Ui ◽

...

Keyword(s):

Cholera Toxin ◽

Pertussis Toxin ◽

Binding Protein ◽

Chemotactic Peptide ◽

Gtp Binding Protein ◽

Peptide Receptor ◽

Adp Ribosylation ◽

Gtp Binding

ADP-ribosylation of bovine S-antigen by cholera toxin

Biochemical and Biophysical Research Communications ◽

10.1016/s0006-291x(88)80754-x ◽

1988 ◽

Vol 156 (3) ◽

pp. 1160-1165 ◽

Cited By ~ 5

Author(s):

Naoka Komori ◽

Maureen A. Rider ◽

Dolores J. Takemoto ◽

Hitoshi Shichi ◽

Hiroyuki Matsumoto

Keyword(s):

Cholera Toxin ◽

Adp Ribosylation

ADP-Ribosylation Factors: A Family of Guanine Nucleotide-Binding Proteins That Activate Cholera Toxin and Regulate Vesicular Transport

Handbook of Natural Toxins, Volume 8 ◽

10.1201/9781482273205-19 ◽

1995 ◽

pp. 285-308

Keyword(s):

Cholera Toxin ◽

Binding Proteins ◽

Vesicular Transport ◽

Nucleotide Binding ◽

Guanine Nucleotide ◽

Adp Ribosylation ◽

Guanine Nucleotide Binding ◽

Nucleotide Binding Proteins ◽

Guanine Nucleotide Binding Proteins

Endogenous and cholera toxin-catalyzed ADP-ribosylation of a plasma membrane protein of RL-PR-C cloned rat hepatocytes

Biochimica et Biophysica Acta (BBA) - General Subjects ◽

10.1016/0304-4165(81)90479-7 ◽

1981 ◽

Vol 673 ◽

pp. 477-486 ◽

Cited By ~ 20

Author(s):

Suzanne K. Beckner ◽

Mevin Blecher

Keyword(s):

Plasma Membrane ◽

Membrane Protein ◽

Cholera Toxin ◽

Rat Hepatocytes ◽

Plasma Membrane Protein ◽

Adp Ribosylation

Separation of the 24 kDa substrate for botulinum C3 ADP-ribosyltransferase and the cholera toxin ADP-ribosylation factor

Biochemical and Biophysical Research Communications ◽

10.1016/s0006-291x(88)80376-0 ◽

1988 ◽

Vol 152 (3) ◽

pp. 957-961 ◽

Cited By ~ 5

Author(s):

Su-Chen Tsai ◽

Ronald Adamik ◽

Joel Moss ◽

Klaus Aktories

Keyword(s):

Cholera Toxin ◽

Adp Ribosylation ◽

Adp Ribosyltransferase ◽

Adp Ribosylation Factor

Effects of temperature on ADP-ribosylation factor stimulation of cholera toxin activity

Biochemistry ◽

10.1021/bi00053a022 ◽

1993 ◽

Vol 32 (2) ◽

pp. 561-566 ◽

Cited By ~ 37

Author(s):

Toshihiko Murayama ◽

Su Chen Tsai ◽

Ronald Adamik ◽

Joel Moss ◽

Martha Vaughan

Keyword(s):

Cholera Toxin ◽

Adp Ribosylation ◽

Effects Of Temperature ◽

Adp Ribosylation Factor ◽

Stimulation Of

The cross-regulation of Gi-protein by cholera toxin involves a phosphorylation by protein kinase A

Biochemical Journal ◽

10.1042/bj3060765 ◽

1995 ◽

Vol 306 (3) ◽

pp. 765-769 ◽

Cited By ~ 6

Author(s):

R Levistre ◽

M Berguerand ◽

G Bereziat ◽

J Masliah

Keyword(s):

Arachidonic Acid ◽

Protein Kinase ◽

Protein Kinase A ◽

Cholera Toxin ◽

Inhibitory Effect ◽

Negative Control ◽

Adp Ribosylation ◽

Gi Proteins ◽

Kinase A

Pretreatment of alveolar macrophages with cholera toxin inhibits the release of arachidonic acid induced by the chemotactic peptide N-formylmethionyl-leucyl-phenylalanine. The results presented here show that cholera toxin might exert its inhibitory effect through the phosphorylation of Gi alpha by protein kinase A (PKA). (1) Gi-proteins from cells pretreated with cholera toxin showed parallel increases in their sensitivity to ADP-ribosylation by toxins in vitro and in Gi alpha phosphorylation. By contrast, the Gi alpha concentration was unchanged. (2) Cholera toxin pretreatment also decreased the functional activity of Gi, as assessed by the inhibition (80%) of agonist-induced binding of guanosine-5′-[gamma-thio]triphosphate (GTP[gamma S]). (3) These effects of cholera toxin were blocked by a specific PKA inhibitor, N-(2-[methyl-amino]ethyl)-3-isoquinolinesulphonamide dihydrochloride (H8) and mimicked by a cyclic AMP (cAMP) analogue and a phosphatase inhibitor. (4) Gi alpha was also phosphorylated in vitro by the catalytic subunit of PKA. In contrast with other cell systems, the stimulation of protein kinase C seems to have no effect on the sensitivity of Gi to ADP-ribosylation or on its phosphorylation. Therefore, the phosphorylation of Gi-proteins by PKA seems to be the actual target of the negative control of arachidonic acid release via the cAMP-mediated pathway.