ArticleProceedings of the National Academy of Sciences of the United States of America1994
Stimulation of endogenous ADP-ribosylation by brefeldin A.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 78 citations in OpenAlex.
- Reversible control of post-Golgi transport by brefeldin A reveals recycling endosome maturation during glycosylphosphatidylinositol-anchored protein transport.Nature communications · 2026Article
- Molecular mechanism of CtBP1-S/BARS-driven membrane fission and its cellular control by metabolic ligands.Science advances · 2026Article
- Quantitative intra-Golgi transport and organization data suggest the stable compartment nature of the Golgi.eLife · 2025Article
- Targeting ADP-ribosylation as an antimicrobial strategy.Biochemical pharmacology · 2019Review
- Beyond glycolysis: GAPDHs are multi-functional enzymes involved in regulation of ROS, autophagy, and plant immune responses.PLoS genetics · 2015Article
- Components of the CtBP1/BARS-dependent fission machinery.Histochemistry and cell biology · 2013Review
- Molecular mechanism and functional role of brefeldin A-mediated ADP-ribosylation of CtBP1/BARS.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Mechanisms of COPI vesicle formation.FEBS letters · 2009Review
- CtBP/BARS: a dual-function protein involved in transcription co-repression and Golgi membrane fission.The EMBO journal · 2003Article
- Functional aspects of protein mono-ADP-ribosylation.The EMBO journal · 2003Review
- Endogenous mono-ADP-ribosylation of the free Gbetagamma prevents stimulation of phosphoinositide 3-kinase-gamma and phospholipase C-beta2 and is activated by G-protein-coupled receptors.The Biochemical journal · 2002Article
- Trichome morphogenesis: a cell-cycle perspective.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2002Review
- The cell morphogenesis gene ANGUSTIFOLIA encodes a CtBP/BARS-like protein and is involved in the control of the microtubule cytoskeleton.The EMBO journal · 2002Article
- Inhibition of secretion by 1,3-Cyclohexanebis(methylamine), a dibasic compound that interferes with coatomer function.Molecular biology of the cell · 1999Article
- Structural basis for the inhibitory effect of brefeldin A on guanine nucleotide-exchange proteins for ADP-ribosylation factors.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Role of brefeldin A-dependent ADP-ribosylation in the control of intracellular membrane transport.Molecular and cellular biochemistry · 1999Article
- Role of NAD+ and ADP-ribosylation in the maintenance of the Golgi structure.The Journal of cell biology · 1997Article
- A mutation in glyceraldehyde 3-phosphate dehydrogenase alters endocytosis in CHO cells.The Journal of cell biology · 1995Article
- Evidence that the 50-kDa substrate of brefeldin A-dependent ADP-ribosylation binds GTP and is modulated by the G-protein beta gamma subunit complex.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Brefeldin A (BFA) is a fungal metabolite that exerts profound and generally inhibitory actions on membrane transport. At least some of the BFA effects are due to inhibition of the GDP-GTP exchange on the ADP-ribosylation factor (ARF) catalyzed by membrane protein(s). ARF activation is likely to be a key event in the association of non-clathrin coat components, including ARF itself, onto transport organelles. ARF, in addition to participating in membrane transport, is known to function as a cofactor in the enzymatic activity of cholera toxin, a bacterial ADP-ribosyltransferase. In this study we have examined whether BFA, in addition to inhibiting membrane transport, might affect endogenous ADP-ribosylation in eukaryotic cells. Two cytosolic proteins of 38 and 50 kDa were enzymatically ADP-ribosylated in the presence of BFA in cellular extracts. The 38-kDa substrate was tentatively identified as the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase. The BFA-binding components mediating inhibition of membrane traffic and stimulation of ADP-ribosylation appear to have the same ligand specificity. These data demonstrate the existence of a BFA-sensitive mono(ADP-ribosyl)transferase that may play a role in membrane movements.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.