Novel phosphorylation states of the yeast spindle pole body
| Autor: | Michael J. MacCoss, Jill M. Hoyt, Alex Zelter, Richard H. Johnson, Trisha N. Davis, Michael Riffle, Kimberly K. Fong, Beth Graczyk |
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| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
QH301-705.5 Science Saccharomyces cerevisiae macromolecular substances Biology Cell cycle medicine.disease_cause General Biochemistry Genetics and Molecular Biology Spindle pole body 03 medical and health sciences 0302 clinical medicine Microtubule γ-tubulin small complex (γ-TuSC) Fluorescence microscope medicine Biology (General) Mitosis 030304 developmental biology Microtubule nucleation 0303 health sciences Mutation Chemistry biology.organism_classification Cell biology 030104 developmental biology Phosphoproteome Spindle pole body (SPB) Phosphorylation General Agricultural and Biological Sciences 030217 neurology & neurosurgery Research Article |
| Zdroj: | Biology Open Biology Open, Vol 7, Iss 10 (2018) |
| ISSN: | 2046-6390 |
| Popis: | Phosphorylation regulates yeast spindle pole body (SPB) duplication and separation and likely regulates microtubule nucleation. We report a phosphoproteomic analysis using tandem mass spectrometry of enriched Saccharomyces cerevisiae SPBs for two cell cycle arrests, G1/S and the mitotic checkpoint, expanding on previously reported phosphoproteomic data sets. We present a novel phosphoproteomic state of SPBs arrested in G1/S by a cdc4-1 temperature-sensitive mutation, with particular focus on phosphorylation events on the γ-tubulin small complex (γ-TuSC). The cdc4-1 arrest is the earliest arrest at which microtubule nucleation has occurred at the newly duplicated SPB. Several novel phosphorylation sites were identified in G1/S and during mitosis on the microtubule nucleating γ-TuSC. These sites were analyzed in vivo by fluorescence microscopy and were shown to be required for proper regulation of spindle length. Additionally, in vivo analysis of two mitotic sites in Spc97 found that phosphorylation of at least one of these sites is required for progression through the cell cycle. This phosphoproteomic data set not only broadens the scope of the phosphoproteome of SPBs, it also identifies several γ-TuSC phosphorylation sites that influence microtubule formation. Summary: A phosphoproteome of yeast spindle pole bodies in G1/S or M phase identifies phosphorylation sites involved in spindle length control and provides direction for future phosphorylation analyses of spindle pole components. |
| Databáze: | OpenAIRE |
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