Storck, E. M. et al. Nat. Chem. https://doi.org/10.1038/s41557-019-0237-6 (2019).
Farnesyl transferase and geranylgeranyl transferase catalyze the attachment of a farnesyl or geranylgeranyl isoprenoid to a C-terminal cysteine motif in an irreversible post-translational process known as protein prenylation. Current approaches to study prenylation have had limited proteome coverage and poor selectivity. Storck et al. introduce a new approach to profile prenylation in cells by using chemical proteomics. They developed a pair of alkyne-containing probes named YnF and TnGG, which are metabolically incorporated into proteins; the alkyne tags allow such modified proteins to be affinity-purified via a click-chemistry reaction. Prenylated proteins can therefore be isolated and identified by liquid chromatography–mass spectrometry. In a human endothelial cell line, Storck et al. identified 80 prenylated proteins, many of which were previously unknown. They also applied the approach to study prenylation of Rab proteins in a mouse model of retinal disease (choroideremia).
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Doerr, A. Probes for protein prenylation. Nat Methods 16, 459 (2019). https://doi.org/10.1038/s41592-019-0446-3
Published:
Issue Date:
DOI: https://doi.org/10.1038/s41592-019-0446-3
This article is cited by
-
Targeting protein modifications in metabolic diseases: molecular mechanisms and targeted therapies
Signal Transduction and Targeted Therapy (2023)