ArticleCell cycle (Georgetown, Tex.)2011
Cell cycle phosphorylation of mitotic exit network (MEN) proteins.
Article in Cell cycle (Georgetown, Tex.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Decoding the Nucleolar Role in Meiotic Recombination and Cell Cycle Control: Insights into Cdc14 Function.International journal of molecular sciences · 2024Review
- The cryo-EM structure of a γ-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems.Nature communications · 2020Article
- The structure and function of deubiquitinases: lessons from budding yeast.Open biology · 2020Review
- A Noncanonical Hippo Pathway Regulates Spindle Disassembly and Cytokinesis During Meiosis inGenetics · 2020Article
- Yeast pericentrin/Spc110 contains multiple domains required for tethering the γ-tubulin complex to the centrosome.Molecular biology of the cell · 2020Article
- Article
- Biochemical analyses reveal amino acid residues critical for cell cycle-dependent phosphorylation of human Cdc14A phosphatase by cyclin-dependent kinase 1.Scientific reports · 2018Article
- TORC1 signaling exerts spatial control over microtubule dynamics by promoting nuclear export of Stu2.The Journal of cell biology · 2017Article
- Temporal and compartment-specific signals coordinate mitotic exit with spindle position.Nature communications · 2017Article
- Reduced kinase activity of polo kinase Cdc5 affects chromosome stability and DNA damage response in S. cerevisiae.Cell cycle (Georgetown, Tex.) · 2016Article
- Cdc14 Early Anaphase Release, FEAR, Is Limited to the Nucleus and Dispensable for Efficient Mitotic Exit.PloS one · 2015Article
- Protein analysis by shotgun/bottom-up proteomics.Chemical reviews · 2013Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Phosphorylation of proteins is an important mechanism used to regulate most cellular processes. Recently, we completed an extensive phosphoproteomic analysis of the core proteins that constitute the Saccharomyces cerevisiae centrosome. Here, we present a study of phosphorylation sites found on the mitotic exit network (MEN) proteins, most of which are associated with the cytoplasmic face of the centrosome. We identified 55 sites on Bfa1, Cdc5, Cdc14 and Cdc15. Eight sites lie in cyclin-dependent kinase motifs (Cdk, S/T-P), and 22 sites are completely conserved within fungi. More than half of the sites were found in centrosomes from mitotic cells, possibly in preparation for their roles in mitotic exit. Finally, we report phosphorylation site information for other important cell cycle and regulatory proteins.
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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.