ArticleCurrent biology : CB2014
Regulation of cyclin-substrate docking by a G1 arrest signaling pathway and the Cdk inhibitor Far1.
Article in Current biology : CB, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 30 citations in OpenAlex.
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- The histone H2B Arg95 residue efficiently recruits the transcription factor Spt16 to mediate Ste5 expression of the pheromone response pathway.Scientific reports · 2023Article
- Phosphorylation of RGS regulates MAP kinase localization and promotes completion of cytokinesis.Life science alliance · 2022Article
- 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
- Comprehensive Analysis of G1 Cyclin Docking Motif Sequences that Control CDK Regulatory Potency In Vivo.Current biology : CB · 2020Article
- Cytoplasmic retention and degradation of a mitotic inducer enable plant infection by a pathogenic fungus.eLife · 2019Article
- MAPK modulation of yeast pheromone signaling output and the role of phosphorylation sites in the scaffold protein Ste5.Molecular biology of the cell · 2019Article
- Analysis of the thresholds for transcriptional activation by the yeast MAP kinases Fus3 and Kss1.Molecular biology of the cell · 2018Article
- Switch-like Transitions Insulate Network Motifs to Modularize Biological Networks.Cell systems · 2016Article
- Compartmentalization of a bistable switch enables memory to cross a feedback-driven transition.Cell · 2015Article
- A docking interface in the cyclin Cln2 promotes multi-site phosphorylation of substrates and timely cell-cycle entry.Current biology : CB · 2015Article
- Docking interactions: cell-cycle regulation and beyond.Current biology : CB · 2014Article
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3 authors at 1 institution in 1 country.
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Abstract
Eukaryotic cell division is often regulated by extracellular signals. In budding yeast, signaling from mating pheromones arrests the cell cycle in G1 phase. This arrest requires the protein Far1, which is thought to antagonize the G1/S transition by acting as a Cdk inhibitor (CKI), although the mechanisms remain unresolved. Recent studies found that G1/S cyclins (Cln1 and Cln2) recognize Cdk substrates via specific docking motifs, which promote substrate phosphorylation in vivo. Here, we show that these docking interactions are inhibited by pheromone signaling and that this inhibition requires Far1. Moreover, Far1 mutants that cannot inhibit docking are defective at cell-cycle arrest. Consistent with this arrest function, Far1 outcompetes substrates for association with G1/S cyclins in vivo, and it is present in large excess over G1/S cyclins during the precommitment period where pheromone can impose G1 arrest. Finally, a comparison of substrates that do and do not require docking suggests that Far1 acts as a multimode inhibitor that antagonizes both kinase activity and substrate recognition by Cln1/2-Cdk complexes. Our findings uncover a novel mechanism of Cdk regulation by external signals and shed new light on Far1 function to provide a revised view of cell-cycle arrest in this model system.
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