ArticleCurrent biology : CB2011
Cyclin-specific docking motifs promote phosphorylation of yeast signaling proteins by G1/S Cdk complexes.
Article in Current biology : CB, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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48 citing papers in PubMed, 73 citations in OpenAlex.
- 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
- High-throughput investigation of cyclin docking interactions reveals the complexity of motif binding determinants.Nature communications · 2025Article
- Phosphate-binding pocket on cyclin B governs CDK substrate phosphorylation and mitotic timing.Nature communications · 2025Article
- SHARK-capture identifies functional motifs in intrinsically disordered protein regions.Protein science : a publication of the Protein Society · 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
- Distinct functional constraints driving conservation of the cofilin N-terminal regulatory tail.Nature communications · 2024Article
- Knockdown of MRPL35 promotes cell apoptosis and inhibits cell proliferation in non-small-cell lung cancer.BMC pulmonary medicine · 2023Article
- CDK signaling via nonconventional CDK phosphorylation sites.Molecular biology of the cell · 2023Review
- A synthetic biology approach reveals diverse and dynamic CDK response profiles via multisite phosphorylation of NLS-NES modules.Science advances · 2022Article
- Article
- Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs.The Biochemical journal · 2022Review
- Multisite phosphorylation by Cdk1 initiates delayed negative feedback to control mitotic transcription.Current biology : CB · 2022Article
- The Eukaryotic Linear Motif resource: 2022 release.Nucleic acids research · 2022Article
- Cyclin/Forkhead-mediated coordination of cyclin waves: an autonomous oscillator rationalizing the quantitative model of Cdk control for budding yeast.NPJ systems biology and applications · 2021Review
- Docking to a Basic Helix Promotes Specific Phosphorylation by G1-Cdk1.International journal of molecular sciences · 2021Article
- Budding yeast relies on GScience advances · 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
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2 authors at 1 institution in 1 country.
Funding
Abstract
backgroundThe eukaryotic cell cycle begins with a burst of cyclin-dependent kinase (Cdk) phosphorylation. In budding yeast, several Cdk substrates are preferentially phosphorylated at the G1/S transition rather than later in the cell cycle when Cdk activity levels are high. These early Cdk substrates include signaling proteins in the pheromone response pathway. Two such proteins, Ste5 and Ste20, are phosphorylated only when Cdk is associated with the G1/S cyclins Cln1 and Cln2 and not G1, S, or M cyclins. The basis of this cyclin specificity is unknown.
resultsHere we show that Ste5 and Ste20 have recognition sequences, or "docking" sites, for the G1/S cyclins. These docking sites, which are distinct from Clb5/cyclin A-binding "RXL" motifs, bind preferentially to Cln2. They strongly enhance Cln2-driven phosphorylation of each substrate in vivo and function largely independent of position and distance to the Cdk sites. We exploited this functional independence to rewire a Cdk regulatory circuit in a way that changes the target of Cdk inhibition in the pheromone response pathway. Furthermore, we uncover functionally active Cln2 docking motifs in several other Cdk substrates. The docking motifs drive cyclin-specific phosphorylation, and the cyclin preference can be switched by using a distinct motif.
conclusionsOur findings indicate that some Cdk substrates are intrinsically capable of being phosphorylated by several different cyclin-Cdk forms, but they are inefficiently phosphorylated in vivo without a cyclin-specific docking site. Docking interactions may play a prevalent but previously unappreciated role in driving phosphorylation of select Cdk substrates preferentially at the G1/S transition.
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