Development of NanoLuc-targeting protein degraders and a universal reporter system to benchmark tag-targeted degradation platforms
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Modulation of protein abundance using t ag- T argeted P rotein D egrader (tTPD) systems targeting FKBP12 F36V (dTAGs) or HaloTag7 (HaloPROTACs) are powerful approaches for preclinical target validation. Interchanging tags and tag-targeting degraders is important to achieve efficient substrate degradation, yet limited degrader/tag pairs are available and side-by-side comparisons have not been performed. To expand the tTPD repertoire we developed catalytic Nano Luc-targeting PRO TACs (NanoTACs) to hijack the CRL4 CRBN complex and degrade NanoLuc tagged substrates, enabling rapid luminescence-based degradation screening. To benchmark NanoTACs against existing tTPD systems we use an interchangeable reporter system to comparatively test optimal degrader/tag pairs. Overall, we find the dTAG system exhibits superior degradation. To align tag-induced degradation with physiology we demonstrate that NanoTACs limit MLKL-driven necroptosis. In this work we extend the tTPD platform to include NanoTACs adding flexibility to tTPD studies, and benchmark each tTPD system to highlight the importance of comparing each system against each substrate.
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Treatment with NanoTAC degraded cells expressing the H-FF-N-F fusion protein, whereas the control compound NC* had no effect.
“Treatment with NanoTAC led to the degradation of cells expressing the H-FF-N-F fusion protein, while the control compound NC* had no effect.”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [547]
NanoTACs effectively recruited the CRL4CRBN E3 ligase complex, leading to degradation of NanoLuc-tagged substrate proteins.
“NanoTACs effectively recruited the CRL4CRBNE3 ligase complex, leading to the degradation of NanoLuc-tagged substrate proteins.”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [547]
NanoTACs acted as catalytic degradation catalysts.
“Furthermore, NanoTACs acted as catalytic degradation catalysts.”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [547]
A hook effect occurred at higher NanoTAC concentrations, preventing degradation because the ligand could not form ternary complexes.
“However, a hook effect was observed at higher concentrations, where degradation was prevented due to the inability of the ligand to form ternary complexes.”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [547]
No studies have been conducted on NanoTACs for undruggable targets.
“Yet, no studies have been conducted on undruggable targets.547”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [547]
NanoTACs are NanoLuc inhibitors bound to E3 ligase ligands that trigger degradation of NanoLuc-labeled proteins of interest.
“NanoTACs are NanoLuc inhibitors bound to E3 ligase ligands, using the complex to trigger the degradation of NanoLuc-labeled POIs.”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [547]
NanoTAC degradation efficiency was concentration-dependent, with NC4 exhibiting the most effective degradation capacity.
“Degradation efficiency was concentration-dependent, with NC4 exhibiting the most effective degradation capacity.”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [547]
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- Authors
- Grohmann, C., Magtoto, C. M., Walker, J. R., Chua, N. K., Gabrielyan, A., Hall, M., Cobbold, S. A., Mieruszynski, S., Brzozowski, M., Simpson, D. S., Dong, H., Dorizzi, B., Jacobsen, A. V., Morrish, E., Silke, N., Murphy, J. M., Heath, J. K., Testa, A., Maniaci, C., Ciulli, A., Lessene, G., Silke, J., & Feltham, R.
- Affiliations
- The University of Melbourne (AU)
- Promega (United States) (US)
- Walter and Eliza Hall Institute of Medical Research (AU)
- Newcastle University (GB)
- University of Dundee (GB)
- Corresponding author
- Feltham, Rebecca
- ORCID
- Grohmann, Christoph
- Magtoto, Charlene M.
- Walker, Joel R.
- Chua, Ngee Kiat
- Cobbold, Simon A.
- Mieruszynski, Stephen
- Brzozowski, Martin
- Simpson, Daniel S.
- Dong, Hao
- Dorizzi, Bridget
- Jacobsen, Annette V.
- Morrish, Emma
- Silke, Natasha
- Murphy, James M.
- Heath, Joan K.
- Testa, Andrea
- Maniaci, Chiara
- Ciulli, Alessio
- Lessene, Guillaume
- Silke, John
- Feltham, Rebecca
- Venue
- Nature Communications
- Published
- 2022-04-19
- Volume
- 13
- Issue
- 1
- Pages
- 2073-2073
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC9019100
- OpenAlex
- W4224291212
- Cited by
- 43
- References
- 42
- Citations by year
- 2026: 10 · 2025: 14 · 2024: 10 · 2023: 8 · 2022: 1
- FWCI
- 2.69
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Discovery Research Portal (University of Dundee) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Minerva Access (University of Melbourne) (submittedVersion, cc-by)
- Newcastle University ePrints (Newcastle Univesity) (cc-by)
- Funders
- Australian Government
- European Commission (ERC-2012-StG-311460)
- State Government of Victoria
- National Health and Medical Research Council (1107149, 9000653, 1172929, 1117089, 1067289)
- 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 › Molecular Biology › CRISPR and Genetic Engineering
- Keywords
- DTAG, target validation, MLKL, necroptosis
- MeSH terms
- Luciferases, Benchmarking, Tacrolimus Binding Protein 1A, Proteolysis
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