ArticleMolecular biology of the cell2016
Chromatin binding of RCC1 during mitosis is important for its nuclear localization in interphase.
Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 19 citations in OpenAlex.
- Multiomic Characterization ofJCO oncology advances · 2025Article
- Ran-GTP assembles a specialized spindle structure for accurate chromosome segregation in medaka early embryos.Nature communications · 2024Article
- PRMT6 methylation of RCC1 regulates mitosis, tumorigenicity, and radiation response of glioblastoma stem cells.Molecular cell · 2021Article
- The Nuclear Mitotic Apparatus (NuMA) Protein: A Key Player for Nuclear Formation, Spindle Assembly, and Spindle Positioning.Frontiers in cell and developmental biology · 2021Review
- Characterization of novel USP6 gene rearrangements in a subset of so-called cellular fibroma of tendon sheath.Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc · 2021Article
- The Multifaceted Roles of RCC1 in Tumorigenesis.Frontiers in molecular biosciences · 2020Review
- RCC1 regulates inner centromeric composition in a Ran-independent fashion.Cell cycle (Georgetown, Tex.) · 2018Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RCC1, a guanine nucleotide exchange factor of the small GTPase Ran, plays various roles throughout the cell cycle. However, the functions of RCC1 in biological processes in vivo are still unclear. In particular, although RCC1 has multifunctional domains, the biological significance of each domain is unclear. To examine each domain of RCC1, we established an RCC1 conditional knockout chicken DT40 cell line and introduced various RCC1 mutants into the knockout cells. We found that nuclear reformation did not occur properly in RCC1-deficient cells and examined whether specific RCC1 mutants could rescue this phenotype. Surprisingly, we found that neither the nuclear localization signal nor the chromatin-binding domain of RCC1 is essential for its function. However, codisruption of these domains resulted in defective nuclear reformation, which was rescued by artificial nuclear localization of RCC1. Our data indicate that chromatin association of RCC1 during mitosis is crucial for its proper nuclear localization in the next interphase. Moreover, proper nuclear localization of RCC1 in interphase is essential for its function through its nucleotide exchange activity.
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