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

Biochemistry ◽  
1993 ◽  
Vol 32 (2) ◽  
pp. 561-566 ◽  
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

scholarly journals Effect of ADP-ribosylation factor amino-terminal deletions on its GTP-dependent stimulation of cholera toxin activity

1994 ◽  
Vol 269 (13) ◽  
pp. 9743-9745
Author(s):  
J.X. Hong ◽  
R.S. Haun ◽  
S.C. Tsai ◽  
J. Moss ◽  
M. Vaughan
Keyword(s):  
Cholera Toxin ◽  
Adp Ribosylation ◽  
Amino Terminal ◽  
Adp Ribosylation Factor ◽  
Stimulation Of

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

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

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

1988 ◽  
Vol 152 (3) ◽  
pp. 957-961 ◽  
Author(s):  
Su-Chen Tsai ◽  
Ronald Adamik ◽  
Joel Moss ◽  
Klaus Aktories
Keyword(s):  
Cholera Toxin ◽  
Adp Ribosylation ◽  
Adp Ribosyltransferase ◽  
Adp Ribosylation Factor

scholarly journals ADP-ribosylation-factor-regulated phospholipase D activity localizes to secretory vesicles and mobilizes to the plasma membrane following N-formylmethionyl-leucyl-phenylalanine stimulation of human neutrophils

1997 ◽  
Vol 325 (3) ◽  
pp. 581-585 ◽  
Author(s):  
C. P. MORGAN ◽  
H. SENGELOV ◽  
J. WHATMORE ◽  
N. BORREGAARD ◽  
S. COCKCROFT
Keyword(s):  
Plasma Membrane ◽  
Phospholipase D ◽  
Small Gtpases ◽  
Human Neutrophils ◽  
Secretory Vesicles ◽  
Rho Proteins ◽  
Adp Ribosylation ◽  
Activated Neutrophils ◽  
Adp Ribosylation Factor ◽  
Stimulation Of

Phospholipase D (PLD) is responsible for the hydrolysis of phosphatidylcholine to produce phosphatidic acid and choline. Human neutrophils contain PLD activity which is regulated by the small GTPases, ADP-ribosylation factor (ARF) and Rho proteins. In this study we have examined the subcellular localization of the ARF-regulated PLD activity in non-activated neutrophils and cells ‘primed‘ with N-formylmethionyl-leucyl-phenylalanine (fMetLeuPhe). We report that PLD activity is localized at the secretory vesicles in control cells and is mobilized to the plasma membrane upon stimulation with fMetLeuPhe. We conclude that the ARF-regulated PLD activity is translocated to the plasma membrane by secretory vesicles upon stimulation of neutrophils with fMetLeuPhe in inflammatory/priming doses. We propose that this relocalization of PLD is important for the subsequent events occurring during neutrophil activation.

scholarly journals The Cholera Toxin A13 Subdomain Is Essential for Interaction with ADP-Ribosylation Factor 6 and Full Toxic Activity but Is Not Required for Translocation from the Endoplasmic Reticulum to the Cytosol

2006 ◽  
Vol 74 (4) ◽  
pp. 2259-2267 ◽  
Author(s):  
Ken Teter ◽  
Michael G. Jobling ◽  
Danielle Sentz ◽  
Randall K. Holmes
Keyword(s):  
Endoplasmic Reticulum ◽  
Cholera Toxin ◽  
Toxic Activity ◽  
Hydrophobic Domain ◽  
Vesicular Traffic ◽  
Adp Ribosylation ◽  
Quality Control Mechanism ◽  
Adp Ribosylation Factor

ABSTRACT Cholera toxin (CT) moves from the plasma membrane to the endoplasmic reticulum (ER) by retrograde vesicular traffic. In the ER, the catalytic CTA1 polypeptide dissociates from the rest of the toxin and enters the cytosol by a process that involves the quality control mechanism of ER-associated degradation (ERAD). The cytosolic CTA1 then ADP ribosylates Gsα, resulting in adenylate cyclase activation and intoxication of the target cell. It is hypothesized that the C-terminal A13 subdomain of CTA1 plays two crucial roles in the intoxication process: (i) it contains a hydrophobic domain that triggers the ERAD mechanism and (ii) it facilitates interaction with the cytosolic ADP-ribosylation factors (ARFs) that serve as allosteric activators of CTA1. In this study, we examined the role(s) of the CTA13 subdomain in CT intoxication. Full-length CTA1 constructs and truncated CTA1 constructs lacking the A13 subdomain were generated and used to conduct two-hybrid studies of interactions with ARF6, in vitro enzyme assays, in vivo toxicity assays, and in vivo processing/degradation assays. Direct, plasmid-mediated expression of CTA1 constructs in the ER or cytosol of transfected CHO cells was used to perform the in vivo assays. With these methods, we found that the A13 subdomain of CTA1 is important both for interaction with ARF6 and for full expression of enzyme activity in vivo. Surprisingly, however, the A13 subdomain was not required for ERAD-mediated passage of CTA1 from the ER to the cytosol. A possible alternative trigger for CTA1 to activate the ERAD mechanism is discussed.

scholarly journals Effects of Arfaptin 1 on Guanine Nucleotide-dependent Activation of Phospholipase D and Cholera Toxin by ADP-ribosylation Factor

1998 ◽  
Vol 273 (33) ◽  
pp. 20697-20701 ◽  
Author(s):  
Su-Chen Tsai ◽  
Ronald Adamik ◽  
Jin-Xin Hong ◽  
Joel Moss ◽  
Martha Vaughan ◽  
...  
Keyword(s):  
Cholera Toxin ◽  
Phospholipase D ◽  
Guanine Nucleotide ◽  
Adp Ribosylation ◽  
Adp Ribosylation Factor

Mechanism of Activation of Cholera Toxin by ADP-Ribosylation Factor (ARF): Both Low- and High-Affinity Interactions of ARF with Guanine Nucleotides Promote Toxin Activation

Biochemistry ◽  
1990 ◽  
Vol 29 (4) ◽  
pp. 855-861 ◽  
Author(s):  
David Bobak ◽  
Matthew Bliziotes ◽  
Masatoshi Noda ◽  
Su-Chen Tsai ◽  
Ronald Adamik ◽  
...  
Keyword(s):  
Cholera Toxin ◽  
Guanine Nucleotides ◽  
Adp Ribosylation ◽  
High Affinity ◽  
Adp Ribosylation Factor
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