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

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 Lett

journal_title

FEBS letters

authors

Thornhill PB,Cohn JB,Drury G,Stanford WL,Bernstein A,Desbarats J

doi

10.1016/j.febslet.2007.08.025

subject

Has Abstract

pub_date

2007-09-18 00:00:00

pages

4455-62

issue

23

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(07)00892-7

journal_volume

581

pub_type

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