ArticleChembiochem : a European journal of chemical biology2017
Small-Molecule-Induced and Cooperative Enzyme Assembly on a 14-3-3 Scaffold.
Article in Chembiochem : a European journal of chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- 14-3-3 Protein-Protein Interactions: From Mechanistic Understanding to Their Small-Molecule Stabilization.Chembiochem : a European journal of chemical biology · 2024Review
- Switchable Control of Scaffold Protein Activity via Engineered Phosphoregulated Autoinhibition.ACS synthetic biology · 2022Article
- Dynamic Protease Activation on a Multimeric Synthetic Protein Scaffold via Adaptable DNA-Based Recruitment Domains.Angewandte Chemie (International ed. in English) · 2021Article
- Designed Asymmetric Protein Assembly on a Symmetric Scaffold.Angewandte Chemie (International ed. in English) · 2020Article
- Conjugated Protein Domains as Engineered Scaffold Proteins.Bioconjugate chemistry · 2020Review
- Modular bioengineered kinase sensorsChemical science · 2020Article
- Proximity-induced caspase-9 activation on a DNA origami-based synthetic apoptosome.Nature catalysis · 2020Article
- Cooperativity basis for small-molecule stabilization of protein-protein interactions.Chemical science · 2019Article
- Cucurbit[8]uril Reactivation of an Inactivated Caspase-8 Mutant Reveals Differentiated Enzymatic Substrate Processing.Chembiochem : a European journal of chemical biology · 2018Article
- Protease-Activatable Scaffold Proteins as Versatile Molecular Hubs in Synthetic Signaling Networks.ACS synthetic biology · 2018Article
- A Binary Bivalent Supramolecular Assembly Platform Based on Cucurbit[8]uril and Dimeric Adapter Protein 14-3-3.Angewandte Chemie (International ed. in English) · 2017Article
- Small-Molecule-Induced and Cooperative Enzyme Assembly on a 14-3-3 Scaffold.Chembiochem : a European journal of chemical biology · 2017Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Scaffold proteins regulate cell signalling by promoting the proximity of putative interaction partners. Although they are frequently applied in cellular settings, fundamental understanding of them in terms of, amongst other factors, quantitative parameters has been lagging behind. Here we present a scaffold protein platform that is based on the native 14-3-3 dimeric protein and is controllable through the action of a small-molecule compound, thus permitting study in an in vitro setting and mathematical description. Robust small-molecule regulation of caspase-9 activity through induced dimerisation on the 14-3-3 scaffold was demonstrated. The individual parameters of this system were precisely determined and used to develop a mathematical model of the scaffolding concept. This model was used to elucidate the strong cooperativity of the enzyme activation mediated by the 14-3-3 scaffold. This work provides an entry point for the long-needed quantitative insights into scaffold protein functioning and paves the way for the optimal use of reengineered 14-3-3 proteins as chemically inducible scaffolds in synthetic systems.
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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.