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. 2020 Feb 26;11:1067. doi: 10.1038/s41467-020-14893-x

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — a In-cell Alkyne probe labeling scheme. b Alk12 labeling is more efficient than Alk14 labeling and NMT inhibition abolishes labeling. c NMT1 but not NMT2 knockdown inhibits lysine myristoylation in HEK293T cells. d NMT1 and NMT2 overexpression produce singly and doubly myristoylated ARF6 based on Alk12 labeling. e Total ion chromatogram from a top–down mass spectrometric analysis that reveals di-myristoylated ARF6 isolated from HEK293T cells with NMT2 overexpression. Confirmatory MS/MS data are found in Supplementary Fig. 4. f Interior pockets (shown as surface) around the NMT2 active site, showing possible channel for second myristoyl (blue arrow) currently occupied by waters (red dots) and glycerol (purple). The surface is colored by the electrostatic properties of the surrounding residues: blue (positive), red (negative), and gray (hydrophobic). The 1.3 σ 2F_O–F_C electron density map is shown as a mesh. g Model of myristoyl-glycine docked in the second pocket, with lysine ready for a second myristoylation reaction.