Imperial College London
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Prof Ed Tate

Faculty of Natural Sciences, Department of Chemistry

GSK Chair in Chemical Biology
 
 
 
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Contact

 

+44 (0)20 7594 3752e.tate Website CV

 
 
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Assistant

 

Ms Agnes Lee +44 (0)20 7594 9852

 
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Location

 

301BMolecular Sciences Research HubWhite City Campus

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Summary

 

Publications

Citation

BibTex format

@article{Ocasio:2024:10.1038/s41587-023-02030-0,
author = {Ocasio, CA and Baggelaar, MP and Sipthorp, J and Losada, de la Lastra A and Tavares, M and Volari, J and Soudy, C and Storck, EM and Houghton, JW and Palma-Duran, SA and MacRae, JI and Tomi, G and Carr, L and Downward, J and Eggert, US and Tate, EW},
doi = {10.1038/s41587-023-02030-0},
journal = {Nature Biotechnology},
title = {A palmitoyl transferase chemical-genetic system to map ZDHHC-specific S-acylation},
url = {http://dx.doi.org/10.1038/s41587-023-02030-0},
year = {2024}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - The 23 human zinc finger Asp-His-His-Cys motif-containing (ZDHHC) S-acyltransferases catalyze long-chain S-acylation at cysteine residues across an extensive network of hundreds of proteins important for normal physiology or dysregulated in disease. Here we present a technology to directly map the protein substrates of a specific ZDHHC at the whole-proteome level, in intact cells. Structure-guided engineering of paired ZDHHC 'hole' mutants and 'bumped' chemically tagged fatty acid probes enabled probe transfer to specific protein substrates with excellent selectivity over wild-type ZDHHCs. Chemical-genetic systems were exemplified for five human ZDHHCs (3, 7, 11, 15 and 20) and applied to generate de novo ZDHHC substrate profiles, identifying >300 substrates and S-acylation sites for new functionally diverse proteins across multiple cell lines. We expect that this platform will elucidate S-acylation biology for a wide range of models and organisms.
AU  - Ocasio,CA
AU  - Baggelaar,MP
AU  - Sipthorp,J
AU  - Losada,de la Lastra A
AU  - Tavares,M
AU  - Volari,J
AU  - Soudy,C
AU  - Storck,EM
AU  - Houghton,JW
AU  - Palma-Duran,SA
AU  - MacRae,JI
AU  - Tomi,G
AU  - Carr,L
AU  - Downward,J
AU  - Eggert,US
AU  - Tate,EW
DO  - 10.1038/s41587-023-02030-0
PY  - 2024///
SN  - 1087-0156
TI  - A palmitoyl transferase chemical-genetic system to map ZDHHC-specific S-acylation
T2  - Nature Biotechnology
UR  - http://dx.doi.org/10.1038/s41587-023-02030-0
UR  - https://www.ncbi.nlm.nih.gov/pubmed/38191663
UR  - https://www.nature.com/articles/s41587-023-02030-0
UR  - http://hdl.handle.net/10044/1/108650
ER  -
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