ArticleCellular signalling2009
Arf GAP2 is positively regulated by coatomer and cargo.
Article in Cellular signalling, 2009. 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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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- An active allosteric mechanism in ASAP1-mediated Arf1 GTP hydrolysis redefines PH domain function.Nature communications · 2025Article
- Article
- Arfs on the Golgi: four conductors, one orchestra.Frontiers in molecular biosciences · 2025Review
- The PH domain in the ArfGAP ASAP1 drives catalytic activation through an unprecedented allosteric mechanism.bioRxiv : the preprint server for biology · 2024Article
- Arf GTPase-activating proteins SMAP1 and AGFG2 regulate the size of Weibel-Palade bodies and exocytosis of von Willebrand factor.Biology open · 2021Article
- Interaction of the N terminus of ADP-ribosylation factor with the PH domain of the GTPase-activating protein ASAP1 requires phosphatidylinositol 4,5-bisphosphate.The Journal of biological chemistry · 2019Article
- Dissection of GTPase-activating proteins reveals functional asymmetry in the COPI coat of budding yeast.Journal of cell science · 2019Article
- ARF GTPases and their GEFs and GAPs: concepts and challenges.Molecular biology of the cell · 2019Review
- 9Å structure of the COPI coat reveals that the Arf1 GTPase occupies two contrasting molecular environments.eLife · 2017Article
- Simple in vitro assay of Arf GAPs and preparation of Arf proteins as substrates.Methods in cell biology · 2015Article
- ArfGAPs: key regulators for receptor sorting.Receptors & clinical investigation · 2014Article
- Retrograde vesicle transport in the Golgi.Protoplasma · 2012Review
- ArfGAP1 function in COPI mediated membrane traffic: currently debated models and comparison to other coat-binding ArfGAPs.Histology and histopathology · 2012Review
- GTP-binding protein-like domain of AGAP1 is protein binding site that allosterically regulates ArfGAP protein catalytic activity.The Journal of biological chemistry · 2012Article
- Models for the functions of Arf GAPs.Seminars in cell & developmental biology · 2011Review
- Dynamic structure of membrane-anchored Arf*GTP.Nature structural & molecular biology · 2010Article
- Arf GAPs: gatekeepers of vesicle generation.FEBS letters · 2010Review
- ACAP-A/B are ArfGAP homologs in dictyostelium involved in sporulation but not in chemotaxis.PloS one · 2010Article
- Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Arf GAP2 is one of four Arf GAPs that function in the Golgi apparatus. We characterized the kinetics of Arf GAP2 and its regulation. Purified Arf GAP2 had little activity compared to purified Arf GAP1. Of the potential regulators we examined, coatomer had the greatest effect, stimulating activity one to two orders of magnitude. The effect was biphasic, with half-maximal activation observed at 50 nM coatomer and activation peaking at approximately 150 nM coatomer. Activation by coatomer was greater for Arf GAP2 than has been reported for Arf GAP1. The effects of phosphoinositides and changes in vesicle curvature on GAP activity were small compared to coatomer; however, both increased coatomer-dependent activity. Peptides from p24 cargo proteins increased Arf GAP2 activity by an additional 2- to 4-fold. The effect of cargo peptide was dependent on coatomer. Overexpressing the cargo protein p25 decreased cellular Arf1*GTP levels. The differential sensitivity of Arf GAP1 and Arf GAP2 to coatomer could coordinate their activities. Based on the common regulatory features of Arf GAP1 and 2, we propose a mechanism for cargo selection in which GTP hydrolysis triggered by cargo binding to the coat protein is coupled to coat polymerization.
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Registered trials
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.