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Nanobody-thioesterase chimeras to specifically target protein palmitoylation
Chien-Wen Kuo1, Caglar Gök1,2, Hannah Fulton1
1School of Cardiovascular & Metabolic Health, College of Medical Veterinary and Life Sciences, University of Glasgow, Glasgow, UK.
Nature Communications
|February 7, 2025
Summary
Researchers developed nanobody-enzyme chimeras to precisely control protein post-translational modifications (PTMs). This method allows targeted manipulation of PTMs, offering potential applications in disease research and clinical settings.
Area of Science:
- Biochemistry
- Molecular Biology
- Cellular Biology
Background:
- Post-translational modifications (PTMs) greatly expand proteome complexity, regulating protein function and cellular processes.
- Dysregulation of PTMs is implicated in numerous diseases, highlighting the need for precise control mechanisms.
Purpose of the Study:
- To develop a novel approach for manipulating PTMs on specific target proteins.
- To demonstrate the ability to control protein depalmitoylation using engineered nanobody-enzyme fusions.
Main Methods:
- Engineered nanobodies fused to thioesterases to specifically remove palmitoyl groups from target proteins.
- Utilized anti-GFP nanobodies for depalmitoylation of GFP-tagged proteins.
- Employed a chemogenetic strategy to enhance nanobody affinity for temporal control.
Main Results:
- Successfully demonstrated targeted depalmitoylation of GFP-tagged substrates using nanobody-thioesterase fusions.
- Showed that manipulating palmitoylation of the Ca(v)1.2 alpha subunit affects channel function and arrhythmia susceptibility in cardiac myocytes.
- Validated the efficacy of nanobody-enzyme chimeras for PTM manipulation.
Conclusions:
- Nanobody-enzyme chimeras offer a versatile platform for specific PTM manipulation.
- This technology has potential applications in fundamental biological research and therapeutic development.
- The approach enables precise control over protein function through targeted modification.
