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Global profiling of dynamic protein palmitoylation

Academic Article
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Overview

authors

  • Martin, B. R.
  • Wang, C.
  • Adibekian, Alexander
  • Tully, S. E.
  • Cravatt, Benjamin

publication date

  • 2012

journal

  • Nature Methods  Journal

abstract

  • The reversible thioester linkage of palmitic acid on cysteines, known as protein S-palmitoylation, facilitates the membrane association and proper subcellular localization of proteins. Here we report the metabolic incorporation of the palmitic acid analog 17-octadecynoic acid (17-ODYA) in combination with stable-isotope labeling with amino acids in cell culture (SILAC) and pulse-chase methods to generate a global quantitative map of dynamic protein palmitoylation events in cells. We distinguished stably palmitoylated proteins from those that turn over rapidly. Treatment with a serine lipase-selective inhibitor identified a pool of dynamically palmitoylated proteins regulated by palmitoyl-protein thioesterases. This subset was enriched in oncoproteins and other proteins linked to aberrant cell growth, migration and cancer. Our method provides a straightforward way to characterize global palmitoylation dynamics in cells and confirms enzyme-mediated depalmitoylation as a critical regulatory mechanism for a specific subset of rapidly cycling palmitoylated proteins.

subject areas

  • Animals
  • Cysteine
  • Fatty Acids, Unsaturated
  • Lipase
  • Lipoylation
  • Mass Spectrometry
  • Mice
  • Organophosphonates
  • Palmitic Acid
  • Protein Processing, Post-Translational
  • Serine Endopeptidases
  • Thiolester Hydrolases
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Identity

PubMed Central ID

  • PMC3248616

International Standard Serial Number (ISSN)

  • 1548-7091

Digital Object Identifier (DOI)

  • 10.1038/nmeth.1769

PubMed ID

  • 22056678
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Additional Document Info

start page

  • 84

end page

  • 89

volume

  • 9

issue

  • 1

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