ArticleProceedings of the National Academy of Sciences of the United States of America2001
A domain unique to plant RanGAP is responsible for its targeting to the plant nuclear rim.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
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Who cites it
69 citing papers in PubMed, 142 citations in OpenAlex.
- Guanine Nucleotide Exchange Factors and Small GTPases: Their Regulation and Functions, Diseases, and Therapeutic Targets.MedComm · 2025Review
- Detailed characterisation of the trypanosome nuclear pore architecture reveals conserved asymmetrical functional hubs that drive mRNA export.PLoS biology · 2025Article
- Genetic control of generative cell shape by DUO1 in Arabidopsis.Plant reproduction · 2023Article
- Dynamic responses of PA to environmental stimuli imaged by a genetically encoded mobilizable fluorescent sensor.Plant communications · 2023Article
- Review
- Molecular and cellular dynamics of early embryonic cell divisions in Volvox carteri.The Plant cell · 2022Article
- Drought stress tolerance mechanisms and their potential common indicators to salinity, insights from the wild watermelonFrontiers in plant science · 2022Review
- Deciphering Precise Gene Transcriptional Expression Using gwINTACT in Tomato.Frontiers in plant science · 2022Article
- Association of RanGAP to nuclear pore complex component, RanBP2/Nup358, is required for pupal development in Drosophila.Cell reports · 2021Article
- Proteomic approach to identify the differentially abundant proteins during flavour development in tuberous roots of3 Biotech · 2021Article
- Meiocyte Isolation by INTACT and Meiotic Transcriptome Analysis inFrontiers in plant science · 2021Article
- Nuclear Transcriptomes at High Resolution Using Retooled INTACT.Plant physiology · 2018Article
- Optimized Methods for the Isolation ofMolecules and cells · 2016Article
- The Small G Protein AtRAN1 Regulates Vegetative Growth and Stress Tolerance in Arabidopsis thaliana.PloS one · 2016Article
- Arabidopsis HIGH PLOIDY2 Sumoylates and Stabilizes Flowering Locus C through Its E3 Ligase Activity.Frontiers in plant science · 2016Article
- Expression and testing in plants of ArcLight, a genetically-encoded voltage indicator used in neuroscience research.BMC plant biology · 2015Article
- Functional characterization of DnSIZ1, a SIZ/PIAS-type SUMO E3 ligase from Dendrobium.BMC plant biology · 2015Article
- GAP Activity, but Not Subcellular Targeting, Is Required for Arabidopsis RanGAP Cellular and Developmental Functions.The Plant cell · 2015Article
- Preprophase band formation and cortical division zone establishment: RanGAP behaves differently from microtubules during their band formation.Plant signaling & behavior · 2015Article
- RAN1 is involved in plant cold resistance and development in rice (Oryza sativa).Journal of experimental botany · 2014Article
9 more citing papers are in PubMed but not listed here.
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2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ran is a small signaling GTPase that is involved in nucleocytoplasmic transport. Two additional functions of animal Ran in the formation of spindle asters and the reassembly of the nuclear envelope in mitotic cells have been recently reported. In contrast to Ras or Rho, Ran is not associated with membranes. Instead, the spatial sequestering of its accessory proteins, the Ran GTPase-activating protein RanGAP and the nucleotide exchange factor RCC1, appears to define the local concentration of RanGTP vs. RanGDP involved in signaling. Mammalian RanGAP is bound to the nuclear pore by a mechanism involving the attachment of small ubiquitin-related modifier protein (SUMO) to its C terminus and the subsequent binding of the SUMOylated domain to the nucleoporin Nup358. Here we show that plant RanGAP utilizes a different mechanism for nuclear envelope association, involving a novel targeting domain that appears to be unique to plants. The N-terminal WPP domain is highly conserved among plant RanGAPs and the small, plant-specific nuclear envelope-associated protein MAF1, but not present in yeast or animal RanGAP. Confocal laser scanning microscopy of green fluorescent protein (GFP) fusion proteins showed that it is necessary for RanGAP targeting and sufficient to target the heterologous protein GFP to the plant nuclear rim. The highly conserved tryptophan and proline residues of the WPP motif are necessary for its function. The 110-aa WPP domain is the first nuclear-envelope targeting domain identified in plants. Its fundamental difference to its mammalian counterpart implies that different mechanisms have evolved in plants and animals to anchor RanGAP at the nuclear surface.
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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.