A novel role of microtubular cytoskeleton in the dynamics of caspase-dependent Fas/CD95 death receptor complexes during apoptosis.

Eszter Doma, Krittalak Chakrabandhu, Anne-Odile Hueber

Equipe labelisée La Ligue; Institute of Signaling, Developmental Biology and Cancer Research, CNRS UMR 6543, Nice, France.

FEBS letters 2010 Mar 5

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The activation of cysteine-aspartic proteases or caspases and the dynamic arrangement of cytoskeletal components are crucial during apoptosis. Here we describe the fate of Fas downstream of the FasL-induced internalization step, including formation of caspase-dependent SDS-stable Fas complexes, which is mediated by cytoskeleton integrity. We show, in particular, that following FasL treatment, the Fas lower aggregate complex can be co-immunoprecipitated with tubulin and an active form of caspase-8 and that this interaction contributes to the propagation of FasL-induced cell death. The importance of cytoskeletal components during FasL-induced apoptosis is highlighted by our detection of a pool of microtubule-associated Fas complexes. Copyright (c) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Citation

Eszter Doma, Krittalak Chakrabandhu, Anne-Odile Hueber. A novel role of microtubular cytoskeleton in the dynamics of caspase-dependent Fas/CD95 death receptor complexes during apoptosis. FEBS letters. 2010 Mar 5;584(5):1033-40