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

Autor:	J, Wenzel, R, Sanzenbacher, M, Ghadimi, M, Lewitzky, Q, Zhou, D R, Kaplan, D, Kabelitz, S M, Feller, O, Janssen
Rok vydání:	2001
Předmět:	Binding Sites Fas Ligand Protein Membrane Glycoproteins T-Lymphocytes Molecular Sequence Data Recombinant Proteins Minor Lymphocyte Stimulatory Antigens Protein Structure Tertiary src Homology Domains Humans Amino Acid Sequence K562 Cells Peptides Protein Binding Signal Transduction
Zdroj:	FEBS letters. 509(2)
ISSN:	0014-5793
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::dccb8fc3bcc6df1f1c8c3e3bd6c5bc09 https://pubmed.ncbi.nlm.nih.gov/11741599 Zobrazit plný text záznamu Plný text