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J Biol Chem, Vol. 273, Issue 22, 13524-13530, May 29, 1998
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From the The onset of apoptosis is coupled to the
proteolytic activation of a family of cysteine proteases, termed
caspases. These proteases cleave their target proteins after an
aspartate residue. Following caspase activation during apoptosis, a
number of specific proteins have been shown to be cleaved. Here we show
that Nedd4, a ubiquitin-protein ligase containing multiple WW domains
and a calcium/lipid-binding domain, is also cleaved during apoptosis induced by a variety of stimuli including Fas-ligation, Hanson Centre for Cancer Research, Institute
of Medical and Veterinary Science, Frome Road, Adelaide, SA 5000, Australia, ¶ Queensland Institute of Medical Research, Post Office
Royal Brisbane Hospital, Herston, Queensland 4029, Australia, and
Center for Apoptosis Research, Kimmel Cancer Institute, Thomas
Jefferson University, Philadelphia, Pennsylvania 19107
-radiation, tumor necrosis factor-
, C-8 ceramide, and etoposide treatment. Extracts from apoptotic cells also generated cleavage patterns similar
to that seen in vivo, and this cleavage was inhibited by an
inhibitor of caspase-3-like proteases. In vitro, Nedd4 was cleaved by a number of caspases, including caspase-1, -3, -6, and -7. By site-directed mutagenesis, one of the in vitro caspase cleavage sites in mouse Nedd4 was mapped to a
DQPD237
sequence, which is conserved between
mouse, rat, and human proteins. This is the first report demonstrating
that an enzyme of the ubiquitin pathway is cleaved by caspases during
apoptosis.
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