ArticleThe Journal of cell biology1996
Spc42p: a phosphorylated component of the S. cerevisiae spindle pole body (SPD) with an essential function during SPB duplication.
Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.
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Who cites it
83 citing papers in PubMed, 154 citations in OpenAlex.
- The B-type cyclin Clb4 prevents meiosis I sister centromere separation in budding yeast.G3 (Bethesda, Md.) · 2025Article
- Yeast centrosomes act as organizing centers to promote Polo kinase-mediated adaptation to persistent DNA damage.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The core spindle pole body scaffold Ppc89 links the pericentrin orthologue Pcp1 to the fission yeast spindle pole body via an evolutionarily conserved interface.Molecular biology of the cell · 2024Article
- Dynamic Live Cell Imaging of Budding Yeast Meiosis.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Meiosis II spindle disassembly requires two distinct pathways.Molecular biology of the cell · 2023Article
- High-throughput genetic screening of meiotic commitment using fluorescence microscopy inSTAR protocols · 2022Article
- Article
- The N-terminus of Sfi1 and yeast centrin Cdc31 provide the assembly site for a new spindle pole body.The Journal of cell biology · 2021Article
- Anatomy of the fungal microtubule organizing center, the spindle pole body.Current opinion in structural biology · 2021Review
- The role of gene dosage in budding yeast centrosome scaling and spontaneous diploidization.PLoS genetics · 2020Article
- Structure and function of Spc42 coiled-coils in yeast centrosome assembly and duplication.Molecular biology of the cell · 2019Article
- Yeast centrosome components form a noncanonical LINC complex at the nuclear envelope insertion site.The Journal of cell biology · 2019Article
- A comprehensive, mechanistically detailed, and executable model of the cell division cycle in Saccharomyces cerevisiae.Nature communications · 2019Article
- Compositional reorganization of the nucleolus in budding yeast mitosis.Molecular biology of the cell · 2019Article
- Key phosphorylation events in Spc29 and Spc42 guide multiple steps of yeast centrosome duplication.Molecular biology of the cell · 2018Article
- Hof1 and Chs4 Interact via F-BAR Domain and Sel1-like Repeats to Control Extracellular Matrix Deposition during Cytokinesis.Current biology : CB · 2017Article
- Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes.The Journal of cell biology · 2017Article
- Aneuploidy Causes Non-genetic Individuality.Cell · 2017Article
- Article
- Kar1 binding to Sfi1 C-terminal regions anchors the SPB bridge to the nuclear envelope.The Journal of cell biology · 2015Article
23 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 42-kD component of the S. cerevisiae spindle pole body (SPB) localizes to the electron-dense central plaque of the SPB. We have cloned the corresponding gene SPC42 (spindle pole component) and show that it is essential. Seven temperature-sensitive (ts) mutants in SPC42 were prepared by error-prone PCR. We found that a change to a proline residue in a potential coiled-coil region of Spc42p was responsible for the ts phenotype in at least three alleles, suggesting that formation of the coiled-coil is essential in normal function. The mutant cells showed a phenotype of predominantly single or bilobed SPBs often with an accumulation of unstructured electron-dense material associated with the bridge structure adjacent to the SPB. This phenotype suggests a defect in SPB duplication. This was confirmed by examining synchronized mutant cells that lose viability when SPB duplication is attempted. Spc42p is a phosphoprotein which shows some cell cycle-regulated phosphorylation. Overexpression of Spc42p causes the formation of a disc- or dome-shaped polymer composed of phosphorylated Spc42p, which is attached to the central plaque and associated with the outer nuclear membrane. Taken together, these data suggest that Spc42p forms a polymeric layer at the periphery of the SPB central plaque which has an essential function during SPB duplication and may facilitate attachment of the SPB to the nuclear membrane.
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