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  3. Dual chemical probes enable quantitative system-wide analysis of protein prenylation and prenylation dynamics

Dual chemical probes enable quantitative system-wide analysis of protein prenylation and prenylation dynamics

  • Nat Chem. 2019 Jun;11(6):552-561. doi: 10.1038/s41557-019-0237-6.
Elisabeth M Storck 1 2,  Julia Morales-Sanfrutos 1 3,  Remigiusz A Serwa 1 4,  Nattawadee Panyain 1,  Thomas Lanyon-Hogg 1,  Tanya Tolmachova 5,  Leandro N Ventimiglia 6,  Juan Martin-Serrano 6,  Miguel C Seabra 5 7,  Beata Wojciak-Stothard 8,  Edward W Tate 9
Affiliations

Affiliations

  • 1 Department of Chemistry, Molecular Sciences Research Hub, Imperial College London, London, UK.
  • 2 Randall Centre for Cell and Molecular Biophysics, School of Basic and Medical Biosciences, King's College London, London, UK.
  • 3 Proteomics Unit, Centre de Regulació Genòmica (CRG), Barcelona Institute of Science and Technology (BIST), Barcelona, Spain.
  • 4 Centre of New Technologies, University of Warsaw, Warsaw, Poland.
  • 5 Molecular Medicine Section, National Heart and Lung Institute, Imperial College London, London, UK.
  • 6 Department of Infectious Diseases, School of Immunology and Microbial Sciences, King's College London, London, UK.
  • 7 CEDOC, NOVA Medical School, Universidade Nova de Lisboa, Lisbon, Portugal.
  • 8 Centre for Pharmacology and Therapeutics, Department of Medicine, Imperial College London, London, UK.
  • 9 Department of Chemistry, Molecular Sciences Research Hub, Imperial College London, London, UK. e.tate@imperial.ac.uk.
PMID: 30936521 DOI: 10.1038/s41557-019-0237-6
Abstract

Post-translational farnesylation or geranylgeranylation at a C-terminal cysteine residue regulates the localization and function of over 100 proteins, including the Ras isoforms, and is a therapeutic target in diseases including Cancer and Infection. Here, we report global and selective profiling of prenylated proteins in living cells enabled by the development of isoprenoid analogues YnF and YnGG in combination with quantitative chemical proteomics. Eighty prenylated proteins were identified in a single human cell line, 64 for the first time at endogenous abundance without metabolic perturbation. We further demonstrate that YnF and YnGG enable direct identification of post-translationally processed prenylated Peptides, proteome-wide quantitative analysis of prenylation dynamics and alternative prenylation in response to four different prenyltransferase inhibitors, and quantification of defective Rab prenylation in a model of the retinal degenerative disease choroideremia.

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