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Multiple interactions of the cytosolic polyproline region of the CD95 ligand: hints for the reverse signal transduction capacity of a death factor 1
Author(s) -
Wenzel Jennifer,
Sanzenbacher Ralf,
Ghadimi Markus,
Lewitzky Marc,
Zhou Qingchun,
Kaplan David R.,
Kabelitz Dieter,
Feller Stephan M.,
Janssen Ottmar
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03174-x
Subject(s) - fas receptor , microbiology and biotechnology , fas ligand , signal transduction , receptor , signal transducing adaptor protein , apoptosis , chemistry , immune system , ligand (biochemistry) , biology , programmed cell death , biochemistry , immunology
The CD95/Fas/Apo‐1 ligand is expressed on activated lymphocytes, NK cells, platelets, certain immune‐privileged cells and some tumor cells and induces apoptosis through the death receptor CD95/Fas/Apo‐1. In murine T cells, membrane‐bound CD95L (Fas ligand) also acts as a costimulatory receptor to coordinate activation and function in vivo. The molecular basis for this reverse signal transduction is yet unknown. In the present report, we identify individual interaction domains of enzymes and adapter molecules that selectively interact with full‐length CD95L from transfectants and human T cells. These results may help to explain the costimulatory capacity of CD95L.