Inhibition of death receptor signals by cellular FLIP View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1997-07

AUTHORS

Martin Irmler, Margot Thome, Michael Hahne, Pascal Schneider, Kay Hofmann, Véronique Steiner, Jean-Luc Bodmer, Michael Schröter, Kim Burns, Chantal Mattmann, Donata Rimoldi, Lars E. French, Jürg Tschopp

ABSTRACT

The widely expressed protein Fas is a member of the tumour necrosis factor receptor family which can trigger apoptosis1. However, Fas surface expression does not necessarily render cells susceptible to Fas ligand-induced death signals1,2, indicating that inhibitors of the apoptosis-signalling pathway must exist. Here we report the characterization of an inhibitor of apoptosis, designated FLIP (for FLICE-inhibitory protein), which is predominantly expressed in muscle and lymphoid tissues. The short form, FLIPS, contains two death effector domains and is structurally related to the viral FLIP inhibitors of apoptosis3, whereas the long form, FLIPL, contains in addition a caspase-like domain in which the active-centre cysteine residue is substituted by a tyrosine residue. FLIPS and FLIPL interact with the adaptor protein FADD4,5 and the protease FLICE6,7, and potently inhibit apoptosis induced by all known human death receptors1. FLIPL is expressed during the early stage of T-cell activation, but disappears when T cells become susceptible to Fas ligand-mediated apoptosis. High levels of FLIPL protein are also detectable in melanoma cell lines and malignant melanoma tumours. Thus FLIP may be implicated in tissue homeostasis as an important regulator of apoptosis. More... »

PAGES

190-195

Journal

TITLE

Nature

ISSUE

6638

VOLUME

388

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/40657

    DOI

    http://dx.doi.org/10.1038/40657

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1027258655

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/9217161


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