The CED-4-homologous protein FLASH is involved in Fas-mediated activation of caspase-8 during apoptosis

Yuzuru Imai, Takaharu Kimura, Akira Murakami, Nobuyuki Yajima, Kazuhiro Sakamaki and Shin Yonehara ()
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Yuzuru Imai: Institute for Virus Research, Kyoto University
Takaharu Kimura: Institute for Virus Research, Kyoto University
Akira Murakami: Institute for Virus Research, Kyoto University
Nobuyuki Yajima: Institute for Virus Research, Kyoto University
Kazuhiro Sakamaki: Institute for Virus Research, Kyoto University
Shin Yonehara: Institute for Virus Research, Kyoto University

Nature, 1999, vol. 398, issue 6730, 777-785

Abstract: Abstract Fas is a cell-surface receptor molecule that relays apoptotic (cell death) signals into cells. When Fas is activated by binding of its ligand, the proteolytic protein caspase-8 is recruited to a signalling complex known as DISC by binding to a Fas-associated adapter protein. A large new protein, FLASH, has now been identified by cloning of its complementary DNA. This protein contains a motif with oligomerizing activity whose sequence is similar to that of the Caenorhabditis elegans protein CED-4, and another domain (DRD domain) that interacts with a death-effector domain in caspase-8 or in the adapter protein. Stimulated Fas binds FLASH, so FLASH is probably a component of the DISC signalling complex. Transient expression of FLASH activates caspase-8, whereas overexpression of a truncated form of FLASH containing only one of its DRD or CED-4-like domains does not allow activation of caspase-8 and Fas-mediated apoptosis to occur. Overexpression of full-length FLASH blocks the anti-apoptotic effect of the adenovirus protein E1B19K. FLASH is therefore necessary for the activation of caspase-8 in Fas-mediated apoptosis.

Date: 1999
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DOI: 10.1038/19709

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