A proteomic screen reveals novel Fas ligand interacting proteins within nervous system Schwann cells
| Autor: | Gillian L. Drury, Julie Desbarats, William L. Stanford, Alan Bernstein, Peter B. Thornhill, Jason B. Cohn |
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| Rok vydání: | 2007 |
| Předmět: |
Proteomics
PACSIN Fas Ligand Protein Proteome Recombinant Fusion Proteins Green Fluorescent Proteins Immunoblotting Molecular Sequence Data Vesicular Transport Proteins Biophysics chemical and pharmacologic phenomena Biology Transfection Endocytosis Biochemistry Fas ligand SH3 domain src Homology Domains Mice Tandem Mass Spectrometry Structural Biology Genetics Animals Humans Immunoprecipitation Adaptor Protein Complex beta Subunits Amino Acid Sequence Molecular Biology Cells Cultured Adaptin β Signal transducing adaptor protein hemic and immune systems Cell Biology Fas receptor Schwann cell Cell biology Death-inducing signaling complex Schwann Cells biological phenomena cell phenomena and immunity Signal transduction Src homology 3 domain Gene Deletion Protein Binding Sorting nexin 18 |
| Zdroj: | FEBS Letters. 581:4455-4462 |
| ISSN: | 0014-5793 |
| Popis: | 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 β, 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. |
| Databáze: | OpenAIRE |
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