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A novel role of microtubular cytoskeleton in the dynamics of caspase‐dependent Fas/CD95 death receptor complexes during apoptosis
Author(s) -
Doma Eszter,
Chakrabandhu Krittalak,
Hueber Anne-Odile
Publication year - 2010
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/j.febslet.2010.01.059
Subject(s) - fas ligand , cytoskeleton , microbiology and biotechnology , fas receptor , apoptosis , internalization , caspase , proteases , microtubule , programmed cell death , caspase 8 , biology , chemistry , receptor , cell , biochemistry , enzyme
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.