ArticleMathematical biosciences2011
Scaffold-mediated nucleation of protein signaling complexes: elementary principles.
Article in Mathematical biosciences, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Synthesis and Characterization of Rubisco-Magnesium Complexes for Potential Gas Adsorption Applications.ACS omega · 2026Article
- Cooperative Free Energy: Induced Protein-Protein Interactions and Cooperative Solvation in Ternary Complexes.Journal of chemical theory and computation · 2025Article
- Lossless single-molecule counting to absolute quantify proteoforms.Scientific reports · 2025Article
- What Makes a Good Protein-Protein Interaction Stabilizer: Analysis and Application of the Dual-Binding Mechanism.ACS central science · 2023Article
- A general model of multivalent binding with ligands of heterotypic subunits and multiple surface receptors.Mathematical biosciences · 2021Article
- Optimal ligand discrimination by asymmetric dimerization and turnover of interferon receptors.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Determinants of Ligand Specificity and Functional Plasticity in Type I Interferon Signaling.Frontiers in immunology · 2021Article
- Designed Asymmetric Protein Assembly on a Symmetric Scaffold.Angewandte Chemie (International ed. in English) · 2020Article
- Article
- Modeling cell line-specific recruitment of signaling proteins to the insulin-like growth factor 1 receptor.PLoS computational biology · 2019Article
- Preassembled GPCR signaling complexes mediate distinct cellular responses to ultralow ligand concentrations.Science signaling · 2018Article
- Small-Molecule-Induced and Cooperative Enzyme Assembly on a 14-3-3 Scaffold.Chembiochem : a European journal of chemical biology · 2017Article
- Absolute Ligand Discrimination by Dimeric Signaling Receptors.Biophysical journal · 2016Article
- Phosphatase specificity and pathway insulation in signaling networks.Biophysical journal · 2015Article
- Glycodendrimers: tools to explore multivalent galectin-1 interactions.Beilstein journal of organic chemistry · 2015Article
- Computational analysis of an autophagy/translation switch based on mutual inhibition of MTORC1 and ULK1.PloS one · 2015Article
- Reconstitution of multivalent PDZ domain binding to the scaffold protein PSD-95 reveals ternary-complex specificity of combinatorial inhibition.Structure (London, England : 1993) · 2014Article
- Multivalent scaffolds induce galectin-3 aggregation into nanoparticles.Beilstein journal of organic chemistry · 2014Article
- A comprehensive mathematical model for three-body binding equilibria.Journal of the American Chemical Society · 2013Article
- Modeling the effect of APC truncation on destruction complex function in colorectal cancer cells.PLoS computational biology · 2013Article
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2 authors.
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Abstract
Proteins with multiple binding sites play important roles in cell signaling systems by nucleating protein complexes in which, for example, enzymes and substrates are co-localized. Proteins that specialize in this function are called by a variety names, including adapter, linker and scaffold. Scaffold-mediated nucleation of protein complexes can be either constitutive or induced. Induced nucleation is commonly mediated by a docking site on a scaffold that is activated by phosphorylation. Here, by considering minimalist mathematical models, which recapitulate scaffold effects seen in more mechanistically detailed models, we obtain analytical and numerical results that provide insights into scaffold function. These results elucidate how recruitment of a pair of ligands to a scaffold depends on the concentrations of the ligands, on the binding constants for ligand-scaffold interactions, on binding cooperativity, and on the milieu of the scaffold, as ligand recruitment is affected by competitive ligands and decoy receptors. For the case of a bivalent scaffold, we obtain an expression for the unique scaffold concentration that maximally recruits a pair of monovalent ligands. Through simulations, we demonstrate that a bivalent scaffold can nucleate distinct sets of ligands to equivalent extents when the scaffold is present at different concentrations. Thus, the function of a scaffold can potentially change qualitatively with a change in copy number. We also demonstrate how a scaffold can change the catalytic efficiency of an enzyme and the sensitivity of the rate of reaction to substrate concentration. The results presented here should be useful for understanding scaffold function and for engineering scaffolds to have desired properties.
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