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Issue 75, 2019
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A hydroxylamine probe for profiling S-acylated fatty acids on proteins

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Abstract

Reversible S-palmitoylation is a key regulatory mechanism of protein function and localization. There is increasing evidence that S-acylation is not restricted to palmitate but it includes shorter, longer, and unsaturated fatty acids. However, the diversity of this protein modification has not been fully explored. Herein, we report a chemical probe that combined with MS-based analysis allows the rapid detection and quantification of fatty acids linked to proteins. We have used this approach to profile the S-acylome and to show that the oncogene N-Ras is heterogeneously acylated with palmitate and palmitoleate. Studies on protein distribution in membrane subdomains with semisynthetic proteins revealed that unsaturated N-Ras presents an increased tendency toward clustering and higher insertion kinetic rate constants.

Graphical abstract: A hydroxylamine probe for profiling S-acylated fatty acids on proteins

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Publication details

The article was received on 01 Aug 2019, accepted on 19 Aug 2019 and first published on 29 Aug 2019


Article type: Communication
DOI: 10.1039/C9CC05989J
Chem. Commun., 2019,55, 11183-11186
  • Open access: Creative Commons BY-NC license
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    A hydroxylamine probe for profiling S-acylated fatty acids on proteins

    J. Schulte-Zweckel, M. Dwivedi, A. Brockmeyer, P. Janning, R. Winter and G. Triola, Chem. Commun., 2019, 55, 11183
    DOI: 10.1039/C9CC05989J

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