Abstract:
: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_name
FEBS Lettjournal_title
FEBS lettersauthors
Thornhill PB,Cohn JB,Drury G,Stanford WL,Bernstein A,Desbarats Jdoi
10.1016/j.febslet.2007.08.025subject
Has Abstractpub_date
2007-09-18 00:00:00pages
4455-62issue
23eissn
0014-5793issn
1873-3468pii
S0014-5793(07)00892-7journal_volume
581pub_type
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