Rapamycin-dependent delocalization as a novel tool to reveal protein-protein interactions in plants
- Author
- Joanna Winkler, Evelien Mylle, Andreas De Meyer, Benjamin Pavie, Julie Merchie, Peter Grones and Daniel Van Damme
- Organization
- Abstract
- Identifying protein-protein interactions (PPI) is crucial to understand any type of biological process. Many PPI tools are available, yet only some function within the context of a plant cell. Narrowing down even further, only few PPI tools allow visualizing higher order interactions. Here, we present a novel and conditional <jats:italic>in vivo</jats:italic> PPI tool for plant research. Knocksideways in plants (KSP) uses the ability of rapamycin to alter the localization of a bait protein and its interactors via the heterodimerization of FKBP and FRB domains. KSP is inherently free from many limitations, which other PPI systems hold. It is an <jats:italic>in vivo</jats:italic> tool, it is flexible concerning the orientation of protein tagging as long as this does not interfere with the interaction and it is compatible with a broad range of fluorophores. KSP is also a conditional tool and therefore does not require additional controls. The interactions can be quantified and in high throughput by the scripts that we provide. Finally, we demonstrate that KSP can visualize higher-order interactions. It is therefore a versatile tool, complementing the PPI methods field with unique characteristics and applications.
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Citation
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-8660704
- MLA
- Winkler, Joanna, et al. “Rapamycin-Dependent Delocalization as a Novel Tool to Reveal Protein-Protein Interactions in Plants.” BioRxiv, 2020, doi:10.1101/2020.03.09.983270.
- APA
- Winkler, J., Mylle, E., De Meyer, A., Pavie, B., Merchie, J., Grones, P., & Van Damme, D. (2020). Rapamycin-dependent delocalization as a novel tool to reveal protein-protein interactions in plants. https://doi.org/10.1101/2020.03.09.983270
- Chicago author-date
- Winkler, Joanna, Evelien Mylle, Andreas De Meyer, Benjamin Pavie, Julie Merchie, Peter Grones, and Daniel Van Damme. 2020. “Rapamycin-Dependent Delocalization as a Novel Tool to Reveal Protein-Protein Interactions in Plants.” BioRxiv. https://doi.org/10.1101/2020.03.09.983270.
- Chicago author-date (all authors)
- Winkler, Joanna, Evelien Mylle, Andreas De Meyer, Benjamin Pavie, Julie Merchie, Peter Grones, and Daniel Van Damme. 2020. “Rapamycin-Dependent Delocalization as a Novel Tool to Reveal Protein-Protein Interactions in Plants.” BioRxiv. doi:10.1101/2020.03.09.983270.
- Vancouver
- 1.Winkler J, Mylle E, De Meyer A, Pavie B, Merchie J, Grones P, et al. Rapamycin-dependent delocalization as a novel tool to reveal protein-protein interactions in plants. bioRxiv. 2020.
- IEEE
- [1]J. Winkler et al., “Rapamycin-dependent delocalization as a novel tool to reveal protein-protein interactions in plants,” bioRxiv. 2020.
@misc{8660704,
abstract = {{Identifying protein-protein interactions (PPI) is crucial to understand any type of biological process. Many PPI tools are available, yet only some function within the context of a plant cell. Narrowing down even further, only few PPI tools allow visualizing higher order interactions. Here, we present a novel and conditional <jats:italic>in vivo</jats:italic> PPI tool for plant research. Knocksideways in plants (KSP) uses the ability of rapamycin to alter the localization of a bait protein and its interactors via the heterodimerization of FKBP and FRB domains. KSP is inherently free from many limitations, which other PPI systems hold. It is an <jats:italic>in vivo</jats:italic> tool, it is flexible concerning the orientation of protein tagging as long as this does not interfere with the interaction and it is compatible with a broad range of fluorophores. KSP is also a conditional tool and therefore does not require additional controls. The interactions can be quantified and in high throughput by the scripts that we provide. Finally, we demonstrate that KSP can visualize higher-order interactions. It is therefore a versatile tool, complementing the PPI methods field with unique characteristics and applications.}},
articleno = {{983270}},
author = {{Winkler, Joanna and Mylle, Evelien and De Meyer, Andreas and Pavie, Benjamin and Merchie, Julie and Grones, Peter and Van Damme, Daniel}},
language = {{eng}},
series = {{bioRxiv}},
title = {{Rapamycin-dependent delocalization as a novel tool to reveal protein-protein interactions in plants}},
url = {{http://doi.org/10.1101/2020.03.09.983270}},
year = {{2020}},
}
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