Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening.

ABSTRACT:

Background

Fas ligand is a cytotoxic effector molecule of T and NK cells which is characterized by an intracellular N-terminal polyproline region that serves as a docking site for SH3 and WW domain proteins. Several previously described Fas ligand-interacting SH3 domain proteins turned out to be crucial for the regulation of storage, expression and function of the death factor. Recent observations, however, indicate that Fas ligand is also subject to posttranslational modifications including shedding and intramembrane proteolysis. This results in the generation of short intracellular fragments that might either be degraded or translocate to the nucleus to influence transcription. So far, protein-protein interactions that specifically regulate the fate of the intracellular fragments

SUBMITTER: Voss M 

PROVIDER: S-EPMC2763855 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature