ArticleMolecular biology of the cell2001
Cnm67p is a spacer protein of the Saccharomyces cerevisiae spindle pole body outer plaque.
Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 50 citations in OpenAlex.
- Meiotic Cytokinesis inJournal of fungi (Basel, Switzerland) · 2024Review
- Anatomy of the fungal microtubule organizing center, the spindle pole body.Current opinion in structural biology · 2021Review
- Analysis of the protein composition of the spindle pole body during sporulation in Ashbya gossypii.PloS one · 2019Article
- Dialogue between centrosomal entrance and exit scaffold pathways regulates mitotic commitment.The Journal of cell biology · 2017Article
- Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes.The Journal of cell biology · 2017Article
- Molecular model of fission yeast centrosome assembly determined by superresolution imaging.The Journal of cell biology · 2017Article
- Article
- A ternary membrane protein complex anchors the spindle pole body in the nuclear envelope in budding yeast.The Journal of biological chemistry · 2017Article
- Article
- The centrosome and its duplication cycle.Cold Spring Harbor perspectives in biology · 2015Review
- A visual screen of protein localization during sporulation identifies new components of prospore membrane-associated complexes in budding yeast.Eukaryotic cell · 2014Article
- Mitotic spindle form and function.Genetics · 2012Article
- Sporulation in the budding yeast Saccharomyces cerevisiae.Genetics · 2011Review
- Structure-function analysis of the C-terminal domain of CNM67, a core component of the Saccharomyces cerevisiae spindle pole body.The Journal of biological chemistry · 2011Article
- Tem1 localization to the spindle pole bodies is essential for mitotic exit and impairs spindle checkpoint function.The Journal of cell biology · 2011Article
- 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
- Membrane assembly modulates the stability of the meiotic spindle-pole body.Journal of cell science · 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
- Mobility, microtubule nucleation and structure of microtubule-organizing centers in multinucleated hyphae of Ashbya gossypii.Molecular biology of the cell · 2010Article
- Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
In Saccharomyces cerevisiae, the spindle pole body (SPB) is the functional homolog of the mammalian centrosome, responsible for the organization of the tubulin cytoskeleton. Cytoplasmic (astral) microtubules essential for the proper segregation of the nucleus into the daughter cell are attached at the outer plaque on the SPB cytoplasmic face. Previously, it has been shown that Cnm67p is an integral component of this structure; cells deleted for CNM67 are lacking the SPB outer plaque and thus experience severe nuclear migration defects. With the use of partial deletion mutants of CNM67, we show that the N- and C-terminal domains of the protein are important for nuclear migration. The C terminus, not the N terminus, is essential for Cnm67p localization to the SPB. On the other hand, only the N terminus is subject to protein phosphorylation of a yet unknown function. Electron microscopy of SPB serial thin sections reveals that deletion of the N- or C-terminal domains disturbs outer plaque formation, whereas mutations in the central coiled-coil domain of Cnm67p change the distance between the SPB core and the outer plaque. We conclude that Cnm67p is the protein that connects the outer plaque to the central plaque embedded in the nuclear envelope, adjusting the space between them by the length of its coiled-coil.
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