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BibTex format

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 = {},
year = {2024}

RIS format (EndNote, RefMan)

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
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