PAPTi: A Peptide Aptamer Interference Toolkit for Perturbation of Protein-Protein Interaction Networks
| Autor: | Johannes T. H. Yeh, Richard Binari, Tenzin Gocha, Ramanuj DasGupta, Norbert Perrimon |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Beta-catenin
Aptamer Dishevelled Proteins Notch signaling pathway Plasma protein binding Article Protein Interaction Mapping Humans Wnt Signaling Pathway beta Catenin Adaptor Proteins Signal Transducing chemistry.chemical_classification Multidisciplinary biology Wnt signaling pathway Signal transducing adaptor protein Phosphoproteins Molecular biology Cell biology Dishevelled HEK293 Cells Notch proteins chemistry biology.protein Aptamers Peptide Protein Binding |
| Zdroj: | Scientific Reports |
| ISSN: | 2045-2322 |
| DOI: | 10.1038/srep01156 |
| Popis: | Signaling proteins often form dynamic protein-protein interaction (PPI) complexes to achieve multi-functionality. Methods to abrogate a subset of PPI interfaces without depleting the full-length protein will be valuable for structure-function relationship annotations. Here, we describe the use of Peptide Aptamer Interference (PAPTi) approach for structure-function network studies. We identified peptide aptamers against Dishevelled (Dsh) and β-catenin (β-cat) to target the Wnt signaling pathway and demonstrate that these FN3-based MONOBODYs (FNDYs) can be used to perturb protein activities both in vitro and in vivo. Further, to investigate the crosstalk between the Wnt and Notch pathways, we isolated FNDYs against the Notch Ankyrin (ANK) region and demonstrate that perturbing the ANK domain of Notch increases the inhibitory activity of Notch towards Wnt signaling. Altogether, these studies demonstrate the power of the PAPTi approach to dissect specific PPI interactions within signaling networks. |
| Databáze: | OpenAIRE |
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