ArticleScience signaling2011
Systematic phosphorylation analysis of human mitotic protein complexes.
Article in Science signaling, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
62 citing papers in PubMed, 109 citations in OpenAlex.
- The TUBG meshwork is associated with centromere dynamics and micronuclear organization.Communications biology · 2026Article
- Molecular requirements for PLK1 activation by T-loop phosphorylation.The EMBO journal · 2026Article
- Phospho-Proteomic Analysis of Interleukin-13 Signaling in Airway Cells Reveals SRC Family Kinase Involvement in Interleukin-13-Induced Inflammatory Responses.International archives of allergy and immunology · 2025Article
- Centromere protection requires strict mitotic inactivation of the Bloom syndrome helicase complex.Nature communications · 2025Article
- Calyculin A Induces Premature Chromosome Condensation and Chromatin Compaction in GbioRxiv : the preprint server for biology · 2025Article
- p31International journal of molecular sciences · 2025Article
- SEC-MX: an approach to systematically study the interplay between protein assembly states and phosphorylation.Nature communications · 2025Article
- Cryo-EM structures of apo-APC/C and APC/CNature communications · 2024Article
- A class I PI3K signalling network regulates primary cilia disassembly in normal physiology and disease.Nature communications · 2024Article
- Article
- Pathogenic mutations in the chromokinesin KIF22 disrupt anaphase chromosome segregation.eLife · 2022Article
- Reconstitution and use of highly active human CDK1:Cyclin-B:CKS1 complexes.Protein science : a publication of the Protein Society · 2022Article
- γ-Tubulin in microtubule nucleation and beyond.Frontiers in cell and developmental biology · 2022Review
- Article
- Molecular insight into how γ-TuRC makes microtubules.Journal of cell science · 2021Review
- The Game of Tubulins.Cells · 2021Review
- The association of Plk1 with the astrin-kinastrin complex promotes formation and maintenance of a metaphase plate.Journal of cell science · 2021Article
- BUB1 and CENP-U, Primed by CDK1, Are the Main PLK1 Kinetochore Receptors in Mitosis.Molecular cell · 2021Article
- Cyclin B3 activates the Anaphase-Promoting Complex/Cyclosome in meiosis and mitosis.PLoS genetics · 2020Article
- Delineation of phenotypes and genotypes related to cohesin structural protein RAD21.Human genetics · 2020Article
2 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
16 authors at 6 institutions in 3 countries.
Funding
Abstract
Progression through mitosis depends on a large number of protein complexes that regulate the major structural and physiological changes necessary for faithful chromosome segregation. Most, if not all, of the mitotic processes are regulated by a set of mitotic protein kinases that control protein activity by phosphorylation. Although many mitotic phosphorylation events have been identified in proteome-scale mass spectrometry studies, information on how these phosphorylation sites are distributed within mitotic protein complexes and which kinases generate these phosphorylation sites is largely lacking. We used systematic protein-affinity purification combined with mass spectrometry to identify 1818 phosphorylation sites in more than 100 mitotic protein complexes. In many complexes, the phosphorylation sites were concentrated on a few subunits, suggesting that these subunits serve as "switchboards" to relay the kinase-regulatory signals within the complexes. Consequent bioinformatic analyses identified potential kinase-substrate relationships for most of these sites. In a subsequent in-depth analysis of key mitotic regulatory complexes with the Aurora kinase B (AURKB) inhibitor Hesperadin and a new Polo-like kinase (PLK1) inhibitor, BI 4834, we determined the kinase dependency for 172 phosphorylation sites on 41 proteins. Combination of the results of the cellular studies with Scansite motif prediction enabled us to identify 14 sites on six proteins as direct candidate substrates of AURKB or PLK1.
Indexed as
Identifiers
What OpenQuestion holds
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.