ArticleCurrent biology : CB2015
A docking interface in the cyclin Cln2 promotes multi-site phosphorylation of substrates and timely cell-cycle entry.
Article in Current biology : CB, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 43 citations in OpenAlex.
- A cyclin-polarity feedback network ensures healthy cell proliferation.Nature communications · 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
- Identification and inhibition of the Cyclin D Rb-docking interface that drives cell division.bioRxiv : the preprint server for biology · 2026Article
- A MAP kinase cascade modulates expression of late G1 phase cyclins in budding yeast.bioRxiv : the preprint server for biology · 2025Article
- Positively charged specificity site in cyclin B1 is essential for mitotic fidelity.Nature communications · 2025Article
- A quantitative intracellular peptide binding assay reveals recognition determinants and context dependence of short linear motifs.bioRxiv : the preprint server for biology · 2024Article
- Whi5 hypo- and hyper-phosphorylation dynamics control cell-cycle entry and progression.Current biology : CB · 2024Article
- Evidence for novel mechanisms that control cell-cycle entry and cell size.Molecular biology of the cell · 2024Article
- Hyperactive Ras disrupts cell size control and a key step in cell cycle entry in budding yeast.Genetics · 2023Article
- G1-Cyclin2 (Cln2) promotes chromosome hypercondensation in eco1/ctf7 rad61 null cells during hyperthermic stress in Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2022Article
- The histone H2B Arg95 residue links the pheromone response pathway to rapamycin-induced GScientific reports · 2022Article
- The Eukaryotic Linear Motif resource: 2022 release.Nucleic acids research · 2022Article
- Bipartite binding of the N terminus of Skp2 to cyclin A.Structure (London, England : 1993) · 2021Article
- Docking to a Basic Helix Promotes Specific Phosphorylation by G1-Cdk1.International journal of molecular sciences · 2021Article
- Budding yeast relies on GScience advances · 2021Article
- Discriminative SKP2 Interactions with CDK-Cyclin Complexes Support a Cyclin A-Specific Role in p27KIP1 Degradation.Journal of molecular biology · 2021Article
- A new linear cyclin docking motif that mediates exclusively S-phase CDK-specific signaling.The EMBO journal · 2021Article
- Cell Biology: Deciphering the ABCs of SLiMs in G1-CDK Signaling.Current biology : CB · 2020Article
- Comprehensive Analysis of G1 Cyclin Docking Motif Sequences that Control CDK Regulatory Potency In Vivo.Current biology : CB · 2020Article
- Proline-Rich Motifs Control G2-CDK Target Phosphorylation and Priming an Anchoring Protein for Polo Kinase Localization.Cell reports · 2020Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
backgroundEukaryotic cell division is driven by cyclin-dependent kinases (CDKs). Distinct cyclin-CDK complexes are specialized to drive different cell-cycle events, though the molecular foundations for these specializations are only partly understood. In budding yeast, the decision to begin a new cell cycle is regulated by three G1 cyclins (Cln1-Cln3). Recent studies revealed that some CDK substrates contain a novel docking motif that is specifically recognized by Cln1 and Cln2, and not by Cln3 or later S- or M-phase cyclins, but the responsible cyclin interface was unknown.
resultsHere, to explore the role of this new docking mechanism in the cell cycle, we first show that it is conserved in a distinct cyclin subtype (Ccn1). Then, we exploit phylogenetic variation to identify cyclin mutations that disrupt docking. These mutations disrupt binding to multiple substrates as well as the ability to use docking sites to promote efficient, multi-site phosphorylation of substrates in vitro. In cells where the Cln2 docking function is blocked, we observed reductions in the polarized morphogenesis of daughter buds and reduced ability to fully phosphorylate the G1/S transcriptional repressor Whi5. Furthermore, disruption of Cln2 docking perturbs the coordination between cell size and division, such that the G1/S transition is delayed.
conclusionsThe findings point to a novel substrate interaction interface on cyclins, with patterns of conservation and divergence that relate to functional distinctions among cyclin subtypes. Furthermore, this docking function helps ensure full phosphorylation of substrates with multiple phosphorylation sites, and this contributes to punctual cell-cycle entry.
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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.