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Site-specific analysis of protein S-acylation by resin-assisted capture.

Publication ,  Journal Article
Forrester, MT; Hess, DT; Thompson, JW; Hultman, R; Moseley, MA; Stamler, JS; Casey, PJ
Published in: J Lipid Res
February 2011

Protein S-acylation is a major posttranslational modification whereby a cysteine thiol is converted to a thioester. A prototype is S-palmitoylation (fatty acylation), in which a protein undergoes acylation with a hydrophobic 16 carbon lipid chain. Although this modification is a well-recognized determinant of protein function and localization, current techniques to study cellular S-acylation are cumbersome and/or technically demanding. We recently described a simple and robust methodology to rapidly identify S-nitrosylation sites in proteins via resin-assisted capture (RAC) and provided an initial description of the applicability of the technique to S-acylated proteins (acyl-RAC). Here we expand on the acyl-RAC assay, coupled with mass spectrometry-based proteomics, to characterize both previously reported and novel sites of endogenous S-acylation. Acyl-RAC should therefore find general applicability in studies of both global and individual protein S-acylation in mammalian cells.

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Published In

J Lipid Res

DOI

EISSN

1539-7262

Publication Date

February 2011

Volume

52

Issue

2

Start / End Page

393 / 398

Location

United States

Related Subject Headings

  • ras Proteins
  • Sepharose
  • Proteins
  • Protein Processing, Post-Translational
  • Lipoylation
  • Electrophoresis, Polyacrylamide Gel
  • Cysteine
  • Biochemistry & Molecular Biology
  • Acylation
  • 3205 Medical biochemistry and metabolomics
 

Citation

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Forrester, M. T., Hess, D. T., Thompson, J. W., Hultman, R., Moseley, M. A., Stamler, J. S., & Casey, P. J. (2011). Site-specific analysis of protein S-acylation by resin-assisted capture. J Lipid Res, 52(2), 393–398. https://doi.org/10.1194/jlr.D011106
Forrester, Michael T., Douglas T. Hess, J Will Thompson, Rainbo Hultman, M Arthur Moseley, Jonathan S. Stamler, and Patrick J. Casey. “Site-specific analysis of protein S-acylation by resin-assisted capture.J Lipid Res 52, no. 2 (February 2011): 393–98. https://doi.org/10.1194/jlr.D011106.
Forrester MT, Hess DT, Thompson JW, Hultman R, Moseley MA, Stamler JS, et al. Site-specific analysis of protein S-acylation by resin-assisted capture. J Lipid Res. 2011 Feb;52(2):393–8.
Forrester, Michael T., et al. “Site-specific analysis of protein S-acylation by resin-assisted capture.J Lipid Res, vol. 52, no. 2, Feb. 2011, pp. 393–98. Pubmed, doi:10.1194/jlr.D011106.
Forrester MT, Hess DT, Thompson JW, Hultman R, Moseley MA, Stamler JS, Casey PJ. Site-specific analysis of protein S-acylation by resin-assisted capture. J Lipid Res. 2011 Feb;52(2):393–398.

Published In

J Lipid Res

DOI

EISSN

1539-7262

Publication Date

February 2011

Volume

52

Issue

2

Start / End Page

393 / 398

Location

United States

Related Subject Headings

  • ras Proteins
  • Sepharose
  • Proteins
  • Protein Processing, Post-Translational
  • Lipoylation
  • Electrophoresis, Polyacrylamide Gel
  • Cysteine
  • Biochemistry & Molecular Biology
  • Acylation
  • 3205 Medical biochemistry and metabolomics