ArticleThe Journal of cell biology1998
Saccharomyces cerevisiae Ndc1p is a shared component of nuclear pore complexes and spindle pole bodies.
Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
79 citing papers in PubMed, 136 citations in OpenAlex.
- Nuclear pore complexes undergo Nup221 exchange during blood-stage asexual replication ofmSphere · 2024Article
- Implications of a multiscale structure of the yeast nuclear pore complex.Molecular cell · 2023Article
- Distinct domains in Ndc1 mediate its interaction with the Nup84 complex and the nuclear membrane.The Journal of cell biology · 2023Article
- Structure, Maintenance, and Regulation of Nuclear Pore Complexes: The Gatekeepers of the Eukaryotic Genome.Cold Spring Harbor perspectives in biology · 2022Review
- Unexplored Cdc42 functions at the budding yeast nucleus suggested by subcellular localization.Small GTPases · 2022Article
- Analysis of the Putative Nucleoporin POM33 in the Filamentous FungusJournal of fungi (Basel, Switzerland) · 2021Article
- Anatomy of the fungal microtubule organizing center, the spindle pole body.Current opinion in structural biology · 2021Review
- Dissecting the Structural Dynamics of the Nuclear Pore Complex.Molecular cell · 2021Article
- A mutation in budding yeastmicroPublication biology · 2021Article
- High-Throughput Identification of Nuclear Envelope Protein Interactions inG3 (Bethesda, Md.) · 2020Article
- The Structure of the Nuclear Pore Complex (An Update).Annual review of biochemistry · 2019Review
- Yeast centrosome components form a noncanonical LINC complex at the nuclear envelope insertion site.The Journal of cell biology · 2019Article
- Expression of TorsinA in a heterologous yeast system reveals interactions with lumenal domains of LINC and nuclear pore complex components.Molecular biology of the cell · 2019Article
- Centrosome Remodelling in Evolution.Cells · 2018Review
- Review
- Stoichiometry and compositional plasticity of the yeast nuclear pore complex revealed by quantitative fluorescence microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Brr6 and Brl1 locate to nuclear pore complex assembly sites to promote their biogenesis.The Journal of cell biology · 2018Article
- Polo-like kinase Cdc5 regulates Spc72 recruitment to spindle pole body in the methylotrophic yeasteLife · 2017Article
- A ternary membrane protein complex anchors the spindle pole body in the nuclear envelope in budding yeast.The Journal of biological chemistry · 2017Article
- Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex.Structure (London, England : 1993) · 2017Article
19 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
We report a novel connection between nuclear pore complexes (NPCs) and spindle pole bodies (SPBs) revealed by our studies of the Saccharomyces cerevisiae NDC1 gene. Although both NPCs and SPBs are embedded in the nuclear envelope (NE) in yeast, their known functions are quite distinct. Previous work demonstrated that NDC1 function is required for proper SPB duplication (Winey, M., M.A. Hoyt, C. Chan, L. Goetsch, D. Botstein, and B. Byers. 1993. J. Cell Biol. 122:743-751). Here, we show that Ndc1p is a membrane protein of the NE that localizes to both NPCs and SPBs. Indirect immunofluorescence microscopy shows that Ndc1p displays punctate, nuclear peripheral localization that colocalizes with a known NPC component, Nup49p. Additionally, distinct spots of Ndc1p localization colocalize with a known SPB component, Spc42p. Immunoelectron microscopy shows that Ndc1p localizes to the regions of NPCs and SPBs that interact with the NE. The NPCs in ndc1-1 mutant cells appear to function normally at the nonpermissive temperature. Finally, we have found that a deletion of POM152, which encodes an abundant but nonessential nucleoporin, suppresses the SPB duplication defect associated with a mutation in the NDC1 gene. We show that Ndc1p is a shared component of NPCs and SPBs and propose a shared function in the assembly of these organelles into the NE.
Indexed as
Identifiers
What OpenQuestion holds
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.