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.
Journal article
2007-09-18T00:00:00+00:00
581
4455 - 4462
7
Adaptor Protein Complex beta Subunits, Amino Acid Sequence, Animals, Cells, Cultured, Fas Ligand Protein, Gene Deletion, Green Fluorescent Proteins, Humans, Immunoblotting, Immunoprecipitation, Mice, Molecular Sequence Data, Protein Binding, Proteome, Proteomics, Recombinant Fusion Proteins, Schwann Cells, Tandem Mass Spectrometry, Transfection, Vesicular Transport Proteins, src Homology Domains