ArticleNature2011
Cascades of multisite phosphorylation control Sic1 destruction at the onset of S phase.
Article in Nature, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 142 papers.
What it found
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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.
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.
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Who cites it
142 citing papers in PubMed, 211 citations in OpenAlex.
- The Small but Versatile Cyclin-Dependent Kinase Subunit CKS: C. elegans CKS-1 Regulates Anaphase Onset and Is Required for Anaphase B During Oocyte Meiosis.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Multi-level precise regulation of gene transcription in the yeast Saccharomyces cerevisiae based on light-sensitive CRISPR/Cas systems.Nucleic acids research · 2026Article
- A cyclin-polarity feedback network ensures healthy cell proliferation.Nature communications · 2026Article
- Chromatin association promotes UBR5-mediated degradation of Rb.bioRxiv : the preprint server for biology · 2026Article
- Correction: Anaphase onset requires CKS-1-mediated destruction of securin in meiosis I and cyclin B1 in meiosis II.The Journal of cell biology · 2026Article
- Microtubules guide Aurora B substrate geometries for accurate chromosome segregation.Science advances · 2026Article
- Decoding Cdk1 control: from mitotic thresholds to meiotic specificity.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2026Review
- Phosphate-binding pocket on cyclin B governs CDK substrate phosphorylation and mitotic timing.Nature communications · 2025Article
- Regulation of centrosome size by the cell-cycle oscillator in Drosophila embryos.The EMBO journal · 2024Article
- Article
- CDK signaling via nonconventional CDK phosphorylation sites.Molecular biology of the cell · 2023Review
- TOR Complex 1: Orchestrating Nutrient Signaling and Cell Cycle Progression.International journal of molecular sciences · 2023Review
- Cyclin-dependent kinases: Masters of the eukaryotic universe.Wiley interdisciplinary reviews. RNA · 2023Review
- Positive feedback induces switch between distributive and processive phosphorylation of Hog1.Nature communications · 2023Article
- Controlling protein stability with SULI, a highly sensitive tag for stabilization upon light induction.Nature communications · 2023Article
- Emerging approaches to CDK inhibitor development, a structural perspective.RSC chemical biology · 2023Article
- Network regulation meets substrate modification chemistry.Journal of the Royal Society, Interface · 2023Article
- Phosphosite Scanning reveals a complex phosphorylation code underlying CDK-dependent activation of Hcm1.Nature communications · 2023Article
- NMR insights into dynamic, multivalent interactions of intrinsically disordered regions: from discrete complexes to condensates.Essays in biochemistry · 2022Article
- An intrinsic temporal order of c-JUN N-terminal phosphorylation regulates its activity by orchestrating co-factor recruitment.Nature communications · 2022Article
82 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
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Multisite phosphorylation of proteins has been proposed to transform a graded protein kinase signal into an ultrasensitive switch-like response. Although many multiphosphorylated targets have been identified, the dynamics and sequence of individual phosphorylation events within the multisite phosphorylation process have never been thoroughly studied. In Saccharomyces cerevisiae, the initiation of S phase is thought to be governed by complexes of Cdk1 and Cln cyclins that phosphorylate six or more sites on the Clb5-Cdk1 inhibitor Sic1, directing it to SCF-mediated destruction. The resulting Sic1-free Clb5-Cdk1 complex triggers S phase. Here, we demonstrate that Sic1 destruction depends on a more complex process in which both Cln2-Cdk1 and Clb5-Cdk1 act in processive multiphosphorylation cascades leading to the phosphorylation of a small number of specific phosphodegrons. The routes of these phosphorylation cascades are shaped by precisely oriented docking interactions mediated by cyclin-specific docking motifs in Sic1 and by Cks1, the phospho-adaptor subunit of Cdk1. Our results indicate that Clb5-Cdk1-dependent phosphorylation generates positive feedback that is required for switch-like Sic1 destruction. Our evidence for a docking network within clusters of phosphorylation sites uncovers a new level of complexity in Cdk1-dependent regulation of cell cycle transitions, and has general implications for the regulation of cellular processes by multisite 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.