A proteomic screen reveals novel Fas ligand interacting proteins within nervous system Schwann cells

FEBS Lett. 2007 Sep 18;581(23):4455-62. doi: 10.1016/j.febslet.2007.08.025. Epub 2007 Aug 22.


Fas ligand (FasL) binds Fas (CD95) to induce apoptosis or activate other signaling pathways. In addition, FasL transduces bidirectional or 'reverse signals'. The intracellular domain of FasL contains consensus sequences for phosphorylation and an extended proline rich region, which regulate its surface expression through undetermined mechanism(s). Here, we used a proteomics approach to identify novel FasL interacting proteins in Schwann cells to investigate signaling through and trafficking of this protein in the nervous system. We identified two novel FasL interacting proteins, sorting nexin 18 and adaptin beta, as well as two proteins previously identified as FasL interacting proteins in T cells, PACSIN2 and PACSIN3. These proteins are all associated with endocytosis and trafficking, highlighting the tight regulation of cell surface expression of FasL in the nervous system.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Protein Complex beta Subunits / metabolism
  • Amino Acid Sequence
  • Animals
  • Cells, Cultured
  • Fas Ligand Protein / analysis
  • Fas Ligand Protein / genetics
  • Fas Ligand Protein / metabolism*
  • Gene Deletion
  • Green Fluorescent Proteins / genetics
  • Green Fluorescent Proteins / metabolism
  • Humans
  • Immunoblotting
  • Immunoprecipitation
  • Mice
  • Molecular Sequence Data
  • Protein Binding
  • Proteome / analysis
  • Proteome / metabolism*
  • Proteomics / methods*
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Schwann Cells / cytology
  • Schwann Cells / metabolism*
  • Tandem Mass Spectrometry
  • Transfection
  • Vesicular Transport Proteins / metabolism
  • src Homology Domains


  • Adaptor Protein Complex beta Subunits
  • Fas Ligand Protein
  • Proteome
  • Recombinant Fusion Proteins
  • Vesicular Transport Proteins
  • Green Fluorescent Proteins