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|Title:||Caspase-mediated cleavage of the ubiquitin-protein ligase Nedd4 during apoptosis|
|Citation:||Journal of Biological Chemistry, 1998; 273(22):13524-13530|
|Publisher:||American Society for Biochemistry and Molecular Biology|
|Kieran F. Harvey, Natasha L. Harvey, Julie M. Michael, Gayathri Parasivam, Nigel Waterhouse, Emad S. Alnemr, Dianne Watters and Sharad Kumar|
|Abstract:||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, γ-radiation, tumor necrosis factor-α, 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.|
Tumor Cells, Cultured
Endosomal Sorting Complexes Required for Transport
Nedd4 Ubiquitin Protein Ligases
|Rights:||© 1998 by The American Society for Biochemistry and Molecular Biology, Inc.|
|Appears in Collections:||Aurora harvest 4|
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