ArticleProceedings of the National Academy of Sciences of the United States of America1995
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.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
14 citing papers in PubMed, 53 citations in OpenAlex.
- Retinoic acid-induced 2 deficiency impairs genomic stability in breast cancer.Breast cancer research : BCR · 2025Article
- ARTC1-mediated VAPB ADP-ribosylation regulates calcium homeostasis.Journal of molecular cell biology · 2024Article
- ARTC1-mediated ADP-ribosylation of GRP78/BiP: a new player in endoplasmic-reticulum stress responses.Cellular and molecular life sciences : CMLS · 2015Article
- 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
- Evidence that mono-ADP-ribosylation of CtBP1/BARS regulates lipid storage.Molecular biology of the cell · 2007Article
- 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
- 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
- Reconstitution of brefeldin A-induced golgi tubulation and fusion with the endoplasmic reticulum in semi-intact chinese hamster ovary cells.Molecular biology of the cell · 2000Article
- 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
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Brefeldin A, a fungal metabolite that inhibits membrane transport, induces the mono(ADP-ribosyl)ation of two cytosolic proteins of 38 and 50 kDa as judged by SDS/PAGE. The 38-kDa substrate has been previously identified as glyceraldehyde-3-phosphate dehydrogenase (GAPDH). We report that the 50-kDa BFA-induced ADP-ribosylated substrate (BARS-50) has native forms of 170 and 130 kDa, as determined by gel filtration of rat brain cytosol, indicating that BARS-50 might exist as a multimeric complex. BARS-50 can bind GTP, as indicated by blot-overlay studies with [alpha-32P]GTP and by photoaffinity labeling with guanosine 5'-[gamma-32P] [beta,gamma-(4-azidoanilido)]triphosphate. Moreover, ADP-ribosylation of BARS-50 was completely inhibited by the beta gamma subunit complex of G proteins, while the ADP-ribosylation of GAPDH was unmodified, indicating that this effect was due to an interaction of the beta gamma complex with BARS-50, rather than with the ADP-ribosylating enzyme. Two-dimensional gel electrophoresis and immunoblot analysis shows that BARS-50 is a group of closely related proteins that appear to be different from all the known GTP-binding proteins.
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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.