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J Biol Chem, Vol. 273, Issue 37, 23621-23624, September 11, 1998
From the Institute of Molecular and Cell Biology, The National
University of Singapore, Singapore 117609, Republic of Singapore
The interleukin-1
-converting enzyme-like
protease precursor, pro-caspase-1, has an N-terminal prodomain that is
removed during cleavage activation of the protease. Here we show that
tumor necrosis factor treatment of HeLa cells induced apoptosis without
detectable proteolytic activation of caspase-1 in the cytosol. Instead,
tumor necrosis factor induced the translocation of pro-caspase-1 to the
nucleus where it was proteolytically activated, releasing the intact
prodomain. We identified a nuclear localization signal in the
prodomain, which was required for translocation of both pro-caspase-1
as well as its prodomain to the nucleus. Surprisingly, transfected
MCF-7 carcinoma or embryonic kidney 293T cells expressing the prodomain
alone underwent apoptosis. These results show that death
signal-induced nuclear targeting is a novel activity of a caspase
prodomain and indicate that caspase-1 and its prodomain may have
hitherto unsuspected nuclear functions in apoptosis.
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