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Related Experiment Videos

Transmembrane TNF (pro-TNF) is palmitoylated.

T Utsumi1, T Takeshige, K Tanaka

  • 1Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Yamaguchi 753-8515, Japan. utsumi@agr.yamaguchi-u.ac.jp

FEBS Letters
|July 4, 2001
PubMed
Summary

Human tumor necrosis factor (pro-TNF) undergoes palmitoylation, a lipid modification. This process attaches palmitic acid to pro-TNF via a thioester bond at Cys-47, anchoring it to the plasma membrane.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Tumor necrosis factor (TNF) is a key cytokine involved in inflammation and immunity.
  • Transmembrane TNF (tmTNF) exists as a precursor form (pro-TNF) before processing.
  • Post-translational modifications like acylation can regulate protein function and localization.

Purpose of the Study:

  • To investigate protein acylation of human transmembrane tumor necrosis factor (pro-TNF).
  • To identify the specific type of acylation and the residue involved in pro-TNF modification.
  • To elucidate the mechanism by which pro-TNF interacts with the plasma membrane.

Main Methods:

  • Expression of human pro-TNF cDNA in COS-1 and Sf9 cells.
  • Metabolic labeling using [(3)H]myristic acid and [(3)H]palmitic acid.

Related Experiment Videos

  • Hydroxylamine treatment to assess thioester bond involvement.
  • Site-directed mutagenesis of cysteine residues in the pro-TNF leader sequence.

    • Main Results:

    • The 26 kDa pro-TNF precursor was specifically labeled with [(3)H]palmitic acid, while the 17 kDa mature TNF was not.
    • Palmitoylation occurred via a thioester bond, as indicated by hydroxylamine sensitivity.
    • Mutagenesis identified Cys-47 as the sole site of palmitoylation, located at the transmembrane/cytoplasmic domain boundary.

    Conclusions:

    • Human pro-TNF undergoes specific palmitoylation at Cys-47.
    • This lipid modification via a thioester bond contributes to pro-TNF's interaction with the plasma membrane.
    • Pro-TNF utilizes both its transmembrane domain and a lipid anchor for membrane association.