ArticleThe Journal of cell biology1997
Control of mitotic events by Nap1 and the Gin4 kinase.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.
What it found
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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.
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.
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Who cites it
80 citing papers in PubMed, 163 citations in OpenAlex.
- Article
- The nucleosome assembly protein Nap1 regulates chromatin stability and nuclear division in Tetrahymena thermophila.Science China. Life sciences · 2026Article
- Mechanisms of growth-dependent regulation of the Gin4 kinase.Molecular biology of the cell · 2025Article
- Nap1 and Kap114 co-chaperone H2A-H2B and facilitate targeted histone release in the nucleus.The Journal of cell biology · 2025Article
- Mechanisms of growth-dependent regulation of the Gin4 kinase.bioRxiv : the preprint server for biology · 2024Article
- Reciprocal regulation by Elm1 and Gin4 controls septin hourglass assembly and remodeling.The Journal of cell biology · 2024Article
- MoNap1, a Nucleosome Assemble Protein 1, Regulates Growth, Development, and Pathogenicity inJournal of fungi (Basel, Switzerland) · 2022Article
- Nutrient availability as an arbiter of cell size.Trends in cell biology · 2022Review
- Article
- Nucleosome Assembly Protein 1, Nap1, Is Required for the Growth, Development, and Pathogenicity ofInternational journal of molecular sciences · 2022Article
- Article
- Growth-Dependent Activation of Protein Kinases Suggests a Mechanism for Measuring Cell Growth.Genetics · 2020Article
- Tsr4 and Nap1, two novel members of the ribosomal protein chaperOME.Nucleic acids research · 2019Article
- Aggregate Filamentous Growth Responses in Yeast.mSphere · 2019Article
- Septin-associated proteins Aim44 and Nis1 traffic between the bud neck and the nucleus in the yeast Saccharomyces cerevisiae.Cytoskeleton (Hoboken, N.J.) · 2019Article
- Effect of Nicotinamide AgainstFrontiers in microbiology · 2019Article
- Article
- The histone chaperone NAP1L3 is required for haematopoietic stem cell maintenance and differentiation.Scientific reports · 2018Article
- Prolonged cyclin-dependent kinase inhibition results in septin perturbations during return to growth and mitosis.The Journal of cell biology · 2018Article
- Characterization of additional components of the environmental pH-sensing complex in the pathogenic fungusThe Journal of biological chemistry · 2018Article
20 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
2 authors at 1 institution in 1 country.
Funding
Abstract
Little is known about the pathways used by cyclins and cyclin-dependent kinases to induce the events of the cell cycle. In budding yeast, a protein called Nap1 binds to the mitotic cyclin Clb2, and Nap1 is required for the ability of Clb2 to induce specific mitotic events, but the role played by Nap1 is unclear. We have used genetic and biochemical approaches to identify additional proteins that function with Nap1 in the control of mitotic events. These approaches have both identified a protein kinase called Gin4 that is required for the ability of Clb2 and Nap1 to promote the switch from polar to isotropic bud growth that normally occurs during mitosis. Gin4 is also required for the ability of Clb2 and Nap1 to promote normal progression through mitosis. The Gin4 protein becomes phosphorylated as cells enter mitosis, resulting in the activation of Gin4 kinase activity, and the phosphorylation of Gin4 is dependent upon Nap1 and Clb2 in vivo. Affinity chromatography experiments demonstrate that Gin4 binds tightly to Nap1, indicating that the functions of these two proteins are closely tied within the cell. These results demonstrate that the activation of Gin4 is under the control of Clb2 and Nap1, and they provide an important step towards elucidating the molecular pathways that link cyclin-dependent kinases to the events they control.
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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.