ArticleMolecular and cellular biology1995
Separate domains of the Ran GTPase interact with different factors to regulate nuclear protein import and RNA processing.
Article in Molecular and cellular biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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
26 citing papers in PubMed, 76 citations in OpenAlex.
- Comparative proteomics reveals different protein expression in platelets in patients with alcoholic liver cirrhosis.Proteome science · 2024Article
- RANBP1 (RAN Binding Protein 1): The Missing Genetic Piece in Cancer Pathophysiology and Other Complex Diseases.Cancers · 2023Review
- Exosome-mediated transfer of CD44 from high-metastatic ovarian cancer cells promotes migration and invasion of low-metastatic ovarian cancer cells.Journal of ovarian research · 2021Article
- Ran GTPase: A Key Player in Tumor Progression and Metastasis.Frontiers in cell and developmental biology · 2020Review
- Intracellular CaCell stem cell · 2019Article
- Ran promotes membrane targeting and stabilization of RhoA to orchestrate ovarian cancer cell invasion.Nature communications · 2019Article
- Article
- Responses to winter dormancy, temperature, and plant hormones share gene networks.Functional & integrative genomics · 2011Article
- RanGTPase: A Key Regulator of Nucleocytoplasmic Trafficking.Molecular and cellular pharmacology · 2009Article
- Contact density affects protein evolutionary rate from bacteria to animals.Journal of molecular evolution · 2008Article
- Phosphorylation of RCC1 in mitosis is essential for producing a high RanGTP concentration on chromosomes and for spindle assembly in mammalian cells.Genes & development · 2004Article
- Cellular functions of TC10, a Rho family GTPase: regulation of morphology, signal transduction and cell growth.Oncogene · 1999Article
- A monoclonal antibody to the COOH-terminal acidic portion of Ran inhibits both the recycling of Ran and nuclear protein import in living cells.The Journal of cell biology · 1999Article
- Highly conserved RNA sequences that are sensors of environmental stress.Molecular and cellular biology · 1998Article
- Viral protein R regulates nuclear import of the HIV-1 pre-integration complex.The EMBO journal · 1998Article
- SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex.The Journal of cell biology · 1998Article
- A T42A Ran mutation: differential interactions with effectors and regulators, and defect in nuclear protein import.Molecular biology of the cell · 1997Article
- Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205-kDa protein and is required for correct nuclear pore assembly.Molecular biology of the cell · 1997Article
- Transportin-mediated nuclear import of heterogeneous nuclear RNP proteins.The Journal of cell biology · 1997Article
- Expression of the murine RanBP1 and Htf9-c genes is regulated from a shared bidirectional promoter during cell cycle progression.The Biochemical journal · 1997Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
Abstract
The small Ras-related GTP binding and hydrolyzing protein Ran has been implicated in a variety of processes, including cell cycle progression, DNA synthesis, RNA processing, and nuclear-cytosolic trafficking of both RNA and proteins. Like other small GTPases, Ran appears to function as a switch: Ran-GTP and Ran-GDP levels are regulated both by guanine nucleotide exchange factors and GTPase activating proteins, and Ran-GTP and Ran-GDP interact differentially with one or more effectors. One such putative effector, Ran-binding protein 1 (RanBP1), interacts selectively with Ran-GTP. Ran proteins contain a diagnostic short, acidic, carboxyl-terminal domain, DEDDDL, which, at least in the case of human Ran, is required for its role in cell cycle regulation. We show here that this domain is required for the interaction between Ran and RanBP1 but not for the interaction between Ran and a Ran guanine nucleotide exchange factor or between Ran and a Ran GTPase activating protein. In addition, Ran lacking this carboxyl-terminal domain functions normally in an in vitro nuclear protein import assay. We also show that RanBP1 interacts with the mammalian homolog of yeast protein RNA1, a protein involved in RNA transport and processing. These results are consistent with the hypothesis that Ran functions directly in at least two pathways, one, dependent on RanBP1, that affects cell cycle progression and RNA export, and another, independent of RanBP1, that affects nuclear protein import.
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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.