ArticleThe EMBO journal1996
Spc110p: assembly properties and role in the connection of nuclear microtubules to the yeast spindle pole body.
Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 83 citations in OpenAlex.
- The γ-TuRC: mastermind of multipurpose actions at the centrosome.Cellular and molecular life sciences : CMLS · 2026Review
- 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
- Yeast pericentrin/Spc110 contains multiple domains required for tethering the γ-tubulin complex to the centrosome.Molecular biology of the cell · 2020Article
- Electron tomography reveals aspects of spindle structure important for mechanical stability at metaphase.Molecular biology of the cell · 2020Article
- Article
- Structure and function of Spc42 coiled-coils in yeast centrosome assembly and duplication.Molecular biology of the cell · 2019Article
- Bridging centrioles and PCM in proper space and time.Essays in biochemistry · 2018Review
- Article
- 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
- Regulation of microtubule nucleation mediated by γ-tubulin complexes.Protoplasma · 2017Review
- Physical determinants of bipolar mitotic spindle assembly and stability in fission yeast.Science advances · 2017Article
- Duplication of the Yeast Spindle Pole Body Once per Cell Cycle.Molecular and cellular biology · 2016Review
- Article
- 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
- Exploring the evolutionary history of centrosomes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014Review
- Biophysics of mitosis.Quarterly reviews of biophysics · 2012Review
- Spindle pole body components are reorganized during fission yeast meiosis.Molecular biology of the cell · 2012Article
- Vesicle docking to the spindle pole body is necessary to recruit the exocyst during membrane formation in Saccharomyces cerevisiae.Molecular biology of the cell · 2010Article
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
Spc110p is an essential component of the budding yeast spindle pole body (SPB). It binds calmodulin and contains a long central coiled-coil rod which acts as a spacer element between the central plaque of the SPB and the ends of the nuclear or spindle microtubules. This suggests that the essential function of Spc110p is to connect the nuclear microtubules to the SPB. To confirm this, we examined the phenotype of ts alleles of SPC110, one of which contains a mutation in the calmodulin binding site and was suppressed by overexpression of calmodulin. The alleles fail to form a functional mitotic spindle because spindle microtubules are not properly connected to the SPB. We also examined the phenotype of the toxic overexpression of either the wild-type or a truncated version of Spc110p containing a deletion of most of the coiled-coil domain. Both of these proteins form large ordered spheroidal polymers in the nucleus. The polymerization of the truncated Spc110p appears to be initiated inside the SPB from the position where Spc110p is normally located, and as the polymer grows in size it severs the connection between the nuclear microtubules and the SPB. The polymers were purified and are composed of Spc110p and calmodulin. A model for the structure of the polymer is proposed.
Indexed as
Identifiers
8887551PMC452189W304139261What 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.