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A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3

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Palmitoylome profiling reveals S-palmitoylation-dependent antiviral activity of IFITM3

Jacob S Yount1, Bruno Moltedo, Yu-Ying Yang

  • 1The Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, New York, USA.

Nature Chemical Biology
|July 6, 2010
PubMed

Insights

Interferon-induced transmembrane protein 3 (IFITM3) antiviral activity is controlled by S-palmitoylation, a lipid modification. This modification regulates IFITM3 clustering and its effectiveness against influenza virus.

Area of Science:

  • Immunology
  • Molecular Biology
  • Virology

Background:

  • Understanding immune effector regulation is key to immunity research.
  • Post-translational modifications significantly influence protein function.

Purpose of the Study:

  • To investigate the post-translational regulation of interferon-induced transmembrane protein 3 (IFITM3).
  • To identify the role of S-palmitoylation in IFITM3's antiviral activity.

Main Methods:

  • Utilized large-scale profiling of palmitoylated proteins in dendritic cells via a chemical reporter strategy.
  • Analyzed the impact of S-palmitoylation on IFITM3 clustering and antiviral function against influenza virus.

Main Results:

  • Discovered over 150 lipid-modified proteins, including those involved in innate immunity.
  • Demonstrated that S-palmitoylation of IFITM3 on specific cysteines controls its membrane clustering and antiviral efficacy.
  • Identified conserved S-palmitoylation sites across the IFITM family.

Conclusions:

  • S-palmitoylation is a critical post-translational modification regulating IFITM3's antiviral activity.
  • This modification is ancient and crucial for host resistance to viral infections.
  • Findings provide insights for understanding IFITM3 function and developing antiviral therapies.

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