ArticleThe Journal of biological chemistry2009
Budding yeast centrosome duplication requires stabilization of Spc29 via Mps1-mediated phosphorylation.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- Key phosphorylation events in Spc29 and Spc42 guide multiple steps of yeast centrosome duplication.Molecular biology of the cell · 2018Article
- Ring closure activates yeast γTuRC for species-specific microtubule nucleation.Nature structural & molecular biology · 2015Article
- Mad1 kinetochore recruitment by Mps1-mediated phosphorylation of Bub1 signals the spindle checkpoint.Genes & development · 2014Article
- Single-step inline hydroxyapatite enrichment facilitates identification and quantitation of phosphopeptides from mass-limited proteomes with MudPIT.Journal of proteome research · 2012Article
- Mitotic spindle form and function.Genetics · 2012Article
- The MPS1 family of protein kinases.Annual review of biochemistry · 2012Review
- A cell cycle phosphoproteome of the yeast centrosome.Science (New York, N.Y.) · 2011Article
- Quantitative mass spectrometry analysis reveals similar substrate consensus motif for human Mps1 kinase and Plk1.PloS one · 2011Article
- Mip1 associates with both the Mps1 kinase and actin, and is required for cell cortex stability and anaphase spindle positioning.Cell cycle (Georgetown, Tex.) · 2011Article
- Native capillary isoelectric focusing for the separation of protein complex isoforms and subcomplexes.Analytical chemistry · 2010Article
- N-terminal regions of Mps1 kinase determine functional bifurcation.The Journal of cell biology · 2010Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Protein phosphorylation plays an important role in the regulation of centrosome duplication. In budding yeast, numerous lines of evidence suggest a requirement for multiple phosphorylation events on individual components of the centrosome to ensure their proper assembly and function. Here, we report the first example of a single phosphorylation event on a component of the yeast centrosome, or spindle pole body (SPB), that is required for SPB duplication and cell viability. This phosphorylation event is on the essential SPB component Spc29 at a conserved Thr residue, Thr(240). Mutation of Thr(240) to Ala is lethal at normal gene dosage, but an increased copy number of this mutant allele results in a conditional phenotype. Phosphorylation of Thr(240) was found to promote the stability of the protein in vivo and is catalyzed in vitro by the Mps1 kinase. Furthermore, the stability of newly synthesized Spc29 is reduced in a mutant strain with reduced Mps1 kinase activity. These results demonstrate the first evidence for a single phosphorylation event on an SPB component that is absolutely required for SPB duplication and suggest that the Mps1 kinase is responsible for this protein-stabilizing phosphorylation.
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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.