ArticleMolecular biology of the cell2005
The organization of the core proteins of the yeast spindle pole body.
Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.
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Who cites it
76 citing papers in PubMed, 122 citations in OpenAlex.
- 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
- Microtubule-associated proteins and motors required for ectopic microtubule array formation in Saccharomyces cerevisiae.Genetics · 2021Article
- 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
- Anatomy of the fungal microtubule organizing center, the spindle pole body.Current opinion in structural biology · 2021Review
- Yeast pericentrin/Spc110 contains multiple domains required for tethering the γ-tubulin complex to the centrosome.Molecular biology of the cell · 2020Article
- The protein architecture of the endocytic coat analyzed by FRET microscopy.Molecular systems biology · 2020Article
- Super-resolution Microscopy-based Bimolecular Fluorescence Complementation to Study Protein Complex Assembly and Co-localization.Bio-protocol · 2020Article
- Mechanisms of chromosome biorientation and bipolar spindle assembly analyzed by computational modeling.eLife · 2020Article
- Electron tomography reveals aspects of spindle structure important for mechanical stability at metaphase.Molecular biology of the cell · 2020Article
- Proximity mapping of the microtubule plus-end tracking protein SLAIN2 using the BioID approach.Turkish journal of biology = Turk biyoloji dergisi · 2020Article
- FRET Microscopy in Yeast.Biosensors · 2019Review
- The huntingtin inclusion is a dynamic phase-separated compartment.Life science alliance · 2019Article
- Structure and function of Spc42 coiled-coils in yeast centrosome assembly and duplication.Molecular biology of the cell · 2019Article
- Theory of Cytoskeletal Reorganization during Cross-Linker-Mediated Mitotic Spindle Assembly.Biophysical journal · 2019Article
- Analysis of the protein composition of the spindle pole body during sporulation in Ashbya gossypii.PloS one · 2019Article
- AI-Assisted Forward Modeling of Biological Structures.Frontiers in cell and developmental biology · 2019Article
- Novel phosphorylation states of the yeast spindle pole body.Biology open · 2018Article
- Increased chromosomal mobility after DNA damage is controlled by interactions between the recombination machinery and the checkpoint.Genes & development · 2018Article
- Centrosome Remodelling in Evolution.Cells · 2018Review
16 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
10 authors at 2 institutions in 1 country.
Funding
Abstract
The spindle pole body (SPB) is the microtubule organizing center of Saccharomyces cerevisiae. Its core includes the proteins Spc42, Spc110 (kendrin/pericentrin ortholog), calmodulin (Cmd1), Spc29, and Cnm67. Each was tagged with CFP and YFP and their proximity to each other was determined by fluorescence resonance energy transfer (FRET). FRET was measured by a new metric that accurately reflected the relative extent of energy transfer. The FRET values established the topology of the core proteins within the architecture of SPB. The N-termini of Spc42 and Spc29, and the C-termini of all the core proteins face the gap between the IL2 layer and the central plaque. Spc110 traverses the central plaque and Cnm67 spans the IL2 layer. Spc42 is a central component of the central plaque where its N-terminus is closely associated with the C-termini of Spc29, Cmd1, and Spc110. When the donor-acceptor pairs were ordered into five broad categories of increasing FRET, the ranking of the pairs specified a unique geometry for the positions of the core proteins, as shown by a mathematical proof. The geometry was integrated with prior cryoelectron tomography to create a model of the interwoven network of proteins within the central plaque. One prediction of the model, the dimerization of the calmodulin-binding domains of Spc110, was confirmed by in vitro analysis.
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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.