Multiple interactions of the cytosolic polyproline region of the CD95 ligand: hints for the reverse signal transduction capacity of a death factor1

FEBS Letters

Janssen, Ottmar⁴  Lewitzky, Marc¹  Kabelitz, Dieter⁴  Kaplan, David R.³  Feller, Stephan M.¹  Wenzel, Jennifer⁴  Sanzenbacher, Ralf⁴  Zhou, Qingchun²  Ghadimi, Markus⁴ 

[1] Cell Signalling Laboratory, Imperial Cancer Research Fund, University of Oxford, Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford, UK;Institute of Organic Synthesis, Center China Normal University, 430079 Wuhan, PR China;Department of Pathology, Case Western Reserve University, 2085 Adelbert Road, Cleveland, OH 44106, USA;Institute for Immunology, Christian-Albrechts-University, Michaelisstraße 5, 24105 Kiel, Germany

关键词: CD95 ligand;    Signal transduction;    Src homology 3 domain;    WW domain;    Protein–protein interaction;    T lymphocyte;    CD95L;    CD95 ligand;    CKI;    casein kinase I;    SH;    Src homology;    TCR;    T cell receptor;    TNF;    tumor necrosis factor;   

DOI  :  10.1016/S0014-5793(01)03174-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown