ArticleMolecular and cellular biology2003
Biochemical characterization of the Ran-RanBP1-RanGAP system: are RanBP proteins and the acidic tail of RanGAP required for the Ran-RanGAP GTPase reaction?
Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 56 citations in OpenAlex.
- The structural basis of RanGAP1 regulation and catalysis in nuclear transport.bioRxiv : the preprint server for biology · 2026Article
- Detailed characterisation of the trypanosome nuclear pore architecture reveals conserved asymmetrical functional hubs that drive mRNA export.PLoS biology · 2025Article
- RANBP17 Overexpression Restores Nucleocytoplasmic Transport and Ameliorates Neurodevelopment in Induced DYT1 Dystonia Motor Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024Article
- Mechanism of exportin retention in the cell nucleus.The Journal of cell biology · 2024Article
- B-type Plexins promote the GTPase activity of Ran to affect androgen receptor nuclear translocation in prostate cancer.Cancer gene therapy · 2023Article
- Article
- Mislocalization of Nucleocytoplasmic Transport Proteins in Human Huntington's Disease PSC-Derived Striatal Neurons.Frontiers in cellular neuroscience · 2021Article
- Ran GTPase: A Key Player in Tumor Progression and Metastasis.Frontiers in cell and developmental biology · 2020Review
- RanBP1 Couples Nuclear Export and Golgi Regulation through LKB1 to Promote Cortical Neuron Polarity.Cell reports · 2018Article
- Comparative interactomics provides evidence for functional specialization of the nuclear pore complex.Nucleus (Austin, Tex.) · 2017Article
- Potential molecular mechanisms for fruiting body formation of Cordyceps illustrated in the case ofMycology · 2017Article
- Interactome Mapping Reveals the Evolutionary History of the Nuclear Pore Complex.PLoS biology · 2016Article
- Lysine-acetylation as a fundamental regulator of Ran function: Implications for signaling of proteins of the Ras-superfamily.Small GTPases · 2015Review
- Small GTP-binding protein Ran is regulated by posttranslational lysine acetylation.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- GAP Activity, but Not Subcellular Targeting, Is Required for Arabidopsis RanGAP Cellular and Developmental Functions.The Plant cell · 2015Article
- The Ran Pathway in Drosophila melanogaster Mitosis.Frontiers in cell and developmental biology · 2015Review
- A structure-based benchmark for protein-protein binding affinity.Protein science : a publication of the Protein Society · 2011Article
- The design of Förster (fluorescence) resonance energy transfer (FRET)-based molecular sensors for Ran GTPase.Methods (San Diego, Calif.) · 2010Review
- GRA proteins of Toxoplasma gondii: maintenance of host-parasite interactions across the parasitophorous vacuolar membrane.The Korean journal of parasitology · 2009Review
- Signaling cascades as cellular devices for spatial computations.Journal of mathematical biology · 2009Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RanBP type proteins have been reported to increase the catalytic efficiency of the RanGAP-mediated GTPase reaction on Ran. Since the structure of the Ran-RanBP1-RanGAP complex showed RanBP1 to be located away from the active site, we reinvestigated the reaction using fluorescence spectroscopy under pre-steady-state conditions. We can show that RanBP1 indeed does not influence the rate-limiting step of the reaction, which is the cleavage of GTP and/or the release of product P(i). It does, however, influence the dynamics of the Ran-RanGAP interaction, its most dramatic effect being the 20-fold stimulation of the already very fast association reaction such that it is under diffusion control (4.5 x 10(8) M(-1) s(-1)). Having established a valuable kinetic system for the interaction analysis, we also found, in contrast to previous findings, that the highly conserved acidic C-terminal end of RanGAP is not required for the switch-off reaction. Rather, genetic experiments in Saccharomyces cerevisiae demonstrate a profound effect of the acidic tail on microtubule organization during mitosis. We propose that the acidic tail of RanGAP is required for a process during mitosis.
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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.