Conditional control of fluorescent protein degradation by an auxin-dependent nanobody
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Abstract
The conditional and reversible depletion of proteins by auxin-mediated degradation is a powerful tool to investigate protein functions in cells and whole organisms. However, its wider applications require fusing the auxin-inducible degron (AID) to individual target proteins. Thus, establishing the auxin system for multiple proteins can be challenging. Another approach for directed protein degradation are anti-GFP nanobodies, which can be applied to GFP stock collections that are readily available in different experimental models. Here, we combine the advantages of auxin and nanobody-based degradation technologies creating an AID-nanobody to degrade GFP-tagged proteins at different cellular structures in a conditional and reversible manner in human cells. We demonstrate efficient and reversible inactivation of the anaphase promoting complex/cyclosome (APC/C) and thus provide new means to study the functions of this essential ubiquitin E3 ligase. Further, we establish auxin degradation in a vertebrate model organism by employing AID-nanobodies in zebrafish.
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Endogenously GFP-tagged proteins in human cells and zebrafish can be degraded in an auxin-inducible manner when co-expressing an AID-anti-GFP nanobody fusion and TIR1.
“In this case, endogenously GFP-tagged proteins in both human cells and zebrafish could be degraded in an auxin-inducible manner, when co-expressing the AID–anti-GFP nanobody fusion as well as TIR1 [29].”
From Advances in targeted degradation of endogenous proteins (2019) · cites this paper as [29]
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- Authors
- Daniel, K., Icha, J., Horenburg, C., Müller, D., Norden, C., & Mansfeld, J.
- Affiliations
- Biotechnologisches Zentrum (DE)
- University of Turku (FI)
- Max Planck Institute of Molecular Cell Biology and Genetics (DE)
- Corresponding author
- Norden, Caren
- Mansfeld, Jörg
- Venue
- Nature Communications
- Published
- 2018-08-17
- Volume
- 9
- Issue
- 1
- Pages
- 3297-3297
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC6098157
- OpenAlex
- W2951829327
- Cited by
- 113
- References
- 45
- Citations by year
- 2026: 9 · 2025: 22 · 2024: 13 · 2023: 9 · 2022: 7 · 2021: 12 · 2020: 23 · 2019: 14 · 2018: 4
- FWCI
- 4.71
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- UTUPub (University of Turku) (submittedVersion, other-oa)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (MA 5831/1-1)
- EC | European Research Council (680042)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Advanced Fluorescence Microscopy Techniques
- Keywords
- auxin-inducible degron, nanobodies, anti-GFP nanobody, anaphase-promoting complex, E3 ubiquitin ligase, zebrafish, human cells
- MeSH terms
- Animals, Cell Compartmentation, HeLa Cells, Humans, Indoleacetic Acids, Kinetics, Lysine, Recombinant Fusion Proteins, Zebrafish, Green Fluorescent Proteins, Proteolysis, Single-Domain Antibodies, Anaphase-Promoting Complex-Cyclosome
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