ArticleMolecular biology of the cell1998
A genetic analysis of interactions with Spc110p reveals distinct functions of Spc97p and Spc98p, components of the yeast gamma-tubulin complex.
Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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39 citing papers in PubMed, 84 citations in OpenAlex.
- CM1-driven assembly and activation of yeast γ-tubulin small complex underlies microtubule nucleation.eLife · 2021Article
- Microtubule pivoting enables mitotic spindle assembly in S. cerevisiae.The Journal of cell biology · 2021Article
- Yeast pericentrin/Spc110 contains multiple domains required for tethering the γ-tubulin complex to the centrosome.Molecular biology of the cell · 2020Article
- Microtubule nucleation by γ-tubulin complexes and beyond.Essays in biochemistry · 2018Review
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- Centrosome Remodelling in Evolution.Cells · 2018Review
- Effect of the Addition ofThe journal of poultry science · 2018Article
- The molecular architecture of the yeast spindle pole body core determined by Bayesian integrative modeling.Molecular biology of the cell · 2017Article
- Direct measurement of the strength of microtubule attachment to yeast centrosomes.Molecular biology of the cell · 2017Article
- Higher-order oligomerization of Spc110p drives γ-tubulin ring complex assembly.Molecular biology of the cell · 2016Article
- Purification of Fluorescently Labeled Saccharomyces cerevisiae Spindle Pole Bodies.Methods in molecular biology (Clifton, N.J.) · 2016Article
- Cell-cycle dependent phosphorylation of yeast pericentrin regulates γ-TuSC-mediated microtubule nucleation.eLife · 2014Article
- GTP regulates the microtubule nucleation activity of γ-tubulin.Nature cell biology · 2013Article
- Article
- An extended γ-tubulin ring functions as a stable platform in microtubule nucleation.The Journal of cell biology · 2012Article
- Mitotic spindle form and function.Genetics · 2012Article
- Article
- Laterally attached kinetochores recruit the checkpoint protein Bub1, but satisfy the spindle checkpoint.Cell cycle (Georgetown, Tex.) · 2010Article
- Structural mutants of the spindle pole body cause distinct alteration of cytoplasmic microtubules and nuclear dynamics in multinucleated hyphae.Molecular biology of the cell · 2010Article
- Fission yeast Pcp1 links polo kinase-mediated mitotic entry to gamma-tubulin-dependent spindle formation.The EMBO journal · 2010Article
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4 authors at 1 institution in 1 country.
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Abstract
The spindle pole body (SPB) in Saccharomyces cerevisiae functions as the microtubule-organizing center. Spc110p is an essential structural component of the SPB and spans between the central and inner plaques of this multilamellar organelle. The amino terminus of Spc110p faces the inner plaque, the substructure from which spindle microtubules radiate. We have undertaken a synthetic lethal screen to identify mutations that enhance the phenotype of the temperature-sensitive spc110-221 allele, which encodes mutations in the amino terminus. The screen identified mutations in SPC97 and SPC98, two genes encoding components of the Tub4p complex in yeast. The spc98-63 allele is synthetic lethal only with spc110 alleles that encode mutations in the N terminus of Spc110p. In contrast, the spc97 alleles are synthetic lethal with spc110 alleles that encode mutations in either the N terminus or the C terminus. Using the two-hybrid assay, we show that the interactions of Spc110p with Spc97p and Spc98p are not equivalent. The N terminus of Spc110p displays a robust interaction with Spc98p in two different two-hybrid assays, while the interaction between Spc97p and Spc110p is not detectable in one strain and gives a weak signal in the other. Extra copies of SPC98 enhance the interaction between Spc97p and Spc110p, while extra copies of SPC97 interfere with the interaction between Spc98p and Spc110p. By testing the interactions between mutant proteins, we show that the lethal phenotype in spc98-63 spc110-221 cells is caused by the failure of Spc98-63p to interact with Spc110-221p. In contrast, the lethal phenotype in spc97-62 spc110-221 cells can be attributed to a decreased interaction between Spc97-62p and Spc98p. Together, these studies provide evidence that Spc110p directly links the Tub4p complex to the SPB. Moreover, an interaction between Spc98p and the amino-terminal region of Spc110p is a critical component of the linkage, whereas the interaction between Spc97p and Spc110p is dependent on Spc98p.
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