ArticleBiophysical journal2013
Measuring affinities of fission yeast spindle pole body proteins in live cells across the cell cycle.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Article
- Analysis of interphase node proteins in fission yeast by quantitative and superresolution fluorescence microscopy.Molecular biology of the cell · 2017Article
- Tension sensors reveal how the kinetochore shares its load.BioEssays : news and reviews in molecular, cellular and developmental biology · 2017Review
- Avoiding artefacts when counting polymerized actin in live cells with LifeAct fused to fluorescent proteins.Nature cell biology · 2016Article
- The septation initiation network controls the assembly of nodes containing Cdr2p for cytokinesis in fission yeast.Journal of cell science · 2015Article
- Characterization of the roles of Blt1p in fission yeast cytokinesis.Molecular biology of the cell · 2014Article
- Every laboratory with a fluorescence microscope should consider counting molecules.Molecular biology of the cell · 2014Article
- Cytokinetic nodes in fission yeast arise from two distinct types of nodes that merge during interphase.The Journal of cell biology · 2014Article
- Determining absolute protein numbers by quantitative fluorescence microscopy.Methods in cell biology · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Characterizing protein-protein interactions is essential for understanding molecular mechanisms, although reproducing cellular conditions in vitro is challenging and some proteins are difficult to purify. We developed a method to measure binding to cellular structures using fission yeast cells as reaction vessels. We varied the concentrations of Sid2p and Mob1p (proteins of the septation initiation network) and measured their binding to spindle pole bodies (SPBs), the centrosome equivalent of yeast. From our measurements we infer that Sid2p and Mob1p both exist as monomeric, heterodimeric, and homodimeric species throughout the cell cycle. During interphase these species have widely different affinities for their common receptor Cdc11p on the SPB. The data support a model with a subset of Cdc11p binding the heterodimeric species with a Kd < 0.1 μM when Sid2p binds Mob1p-Cdc11p and Kd in the micromolar range when Mob1p binds Sid2p-Cdc11p. During mitosis an additional species presumed to be the phosphorylated Sid2p-Mob1p heterodimer binds SPBs with a lower affinity. Homodimers of Sid2p or Mob1p bind to the rest of Cdc11p at SPBs with lower affinity: Kds > 10 μM during interphase and somewhat stronger during mitosis. These measurements allowed us to account for the fluctuations in Sid2p binding to SPBs throughout the cell cycle.
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