ArticleMolecular biology of the cell1997
A mutational analysis identifies three functional regions of the spindle pole component Spc110p in Saccharomyces cerevisiae.
Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Condensation of pericentrin proteins in human cells illuminates phase separation in centrosome assembly.Journal of cell science · 2021Article
- Key phosphorylation events in Spc29 and Spc42 guide multiple steps of yeast centrosome duplication.Molecular biology of the cell · 2018Article
- Studying Spatial Protein Quality Control, Proteopathies, and Aging Using Different Model Misfolding Proteins inFrontiers in molecular neuroscience · 2018Review
- The molecular architecture of the yeast spindle pole body core determined by Bayesian integrative modeling.Molecular biology of the cell · 2017Article
- Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes.The Journal of cell biology · 2017Article
- Direct measurement of the strength of microtubule attachment to yeast centrosomes.Molecular biology of the cell · 2017Article
- The centrosome and its duplication cycle.Cold Spring Harbor perspectives in biology · 2015Review
- Ring closure activates yeast γTuRC for species-specific microtubule nucleation.Nature structural & molecular biology · 2015Article
- Cell-cycle dependent phosphorylation of yeast pericentrin regulates γ-TuSC-mediated microtubule nucleation.eLife · 2014Article
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- Pericentrin in cellular function and disease.The Journal of cell biology · 2010Review
- A molecular mechanism of temperature sensitivity for mutations affecting the Drosophila muscle regulator Myocyte enhancer factor-2.Genetics · 2009Article
- Requirement for the budding yeast polo kinase Cdc5 in proper microtubule growth and dynamics.Eukaryotic cell · 2008Article
- The structure of the gamma-tubulin small complex: implications of its architecture and flexibility for microtubule nucleation.Molecular biology of the cell · 2008Article
- Ppc89 links multiple proteins, including the septation initiation network, to the core of the fission yeast spindle-pole body.Molecular biology of the cell · 2006Article
- A high-efficiency method to replace essential genes with mutant alleles in yeast.Yeast (Chichester, England) · 2005Article
- The nuclear pore complex-associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly.The Journal of cell biology · 2005Article
- The organization of the core proteins of the yeast spindle pole body.Molecular biology of the cell · 2005Article
- Analysis of a spindle pole body mutant reveals a defect in biorientation and illuminates spindle forces.Molecular biology of the cell · 2005Article
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2 authors.
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Abstract
The central coiled coil of the essential spindle pole component Spc110p spans the distance between the central and inner plaques of the Saccharomyces cerevisiae spindle pole body (SPB). The carboxy terminus of Spc110p, which binds calmodulin, resides at the central plaque, and the amino terminus resides at the inner plaque from which nuclear microtubules originate. To dissect the functions of Spc110p, we created temperature-sensitive mutations in the amino and carboxy termini. Analysis of the temperature-sensitive spc110 mutations and intragenic complementation analysis of the spc110 alleles defined three functional regions of Spc110p. Region I is located at the amino terminus. Region II is located at the carboxy-terminal end of the coiled coil, and region III is the previously defined calmodulin-binding site. Overexpression of SPC98 suppresses the temperature sensitivity conferred by mutations in region I but not the phenotypes conferred by mutations in the other two regions, suggesting that the amino terminus of Spc110p is involved in an interaction with the gamma-tubulin complex composed of Spc97p, Spc98p, and Tub4p. Mutations in region II lead to loss of SPB integrity during mitosis, suggesting that this region is required for the stable attachment of Spc110p to the central plaque. Our results strongly argue that Spc110p links the gamma-tubulin complex to the central plaque of the SPB.
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