RGD Reference Report - Binding of the intracellular Fas ligand (FasL) domain to the adaptor protein PSTPIP results in a cytoplasmic localization of FasL. - Rat Genome Database

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Binding of the intracellular Fas ligand (FasL) domain to the adaptor protein PSTPIP results in a cytoplasmic localization of FasL.

Authors: Baum, W  Kirkin, V  Fernandez, SB  Pick, R  Lettau, M  Janssen, O  Zornig, M 
Citation: Baum W, etal., J Biol Chem. 2005 Dec 2;280(48):40012-24. Epub 2005 Oct 4.
RGD ID: 1582442
Pubmed: PMID:16204241   (View Abstract at PubMed)
DOI: DOI:10.1074/jbc.M502222200   (Journal Full-text)

The tumor necrosis factor family member Fas ligand (FasL) induces apoptosis in Fas receptor-expressing target cells and is an important cytotoxic effector molecule used by CTL- and NK-cells. In these hematopoietic cells, newly synthesized FasL is stored in specialized secretory lysosomes and only delivered to the cell surface upon activation and target cell recognition. FasL contains an 80-amino acid-long cytoplasmic tail, which includes a proline-rich domain as a bona fide Src homology 3 domain-binding site. This proline-rich domain has been implicated in FasL sorting to secretory lysosomes, and it may also be important for reverse signaling via FasL, which has been described to influence T-cell activation. Here we report the identification of the Src homology 3 domain-containing adaptor protein PSTPIP as a FasL-interacting partner, which binds to the proline-rich domain. PSTPIP co-expression leads to an increased intracellular localization of Fas ligand, thereby regulating extracellular availability and cytotoxic activity of the molecule. In addition, we demonstrate recruitment of the tyrosine phosphatase PTP-PEST by PSTPIP into FasL.PSTPIP.PTP-PEST complexes which may contribute to FasL reverse signaling.

Objects referenced in this article
Gene Faslg Fas ligand Rattus norvegicus

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