Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/8923
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Type: Journal article
Title: Dimerization and auto processing of the Nedd2 (caspase 2) precursor requires both the prodomain and the carboxyl-terminal regions
Author: Butt, A.
Harvey, N.
Parasivam, G.
Kumar, S.
Citation: Journal of Biological Chemistry, 1998; 273(12):6763-6768
Publisher: American Society for Biochemistry and Molecular Biology
Issue Date: 1998
ISSN: 1083-351X
1083-351X
Statement of
Responsibility: 
Alison J. Butt, Natasha L. Harvey, Gayathri Parasivam and Sharad Kumar
Abstract: Nedd2 (caspase-2) is a cysteine protease of the caspase family that has been demonstrated to play a role in the apoptotic pathway. The 51-kDa precursor of Nedd2 undergoes cleavage into two subunits following various apoptotic stimuli. In this study, we have investigated the dimerization of the Nedd2 precursor (pro-Nedd2) in Saccharomyces cerevisiae and its self-processing activity in vivo. We demonstrate that the expression of pro-Nedd2 in yeast cells results in processing of the precursor. A catalytically inactive pro-Nedd2 mutant dimerized in yeast, and the dimerization required both the prodomain and the carboxyl-terminal residues. Aspartate mutants that block the removal of the p14/p12 subunits, but not the wild-type Nedd2, were shown to dimerize in yeast cells, suggesting that dimerization occurs prior to processing. In vitro processing of pro-Nedd2 by recombinant active Nedd2 defined the aspartate residues that are crucial for processing to occur. Both the in vivo and in vitro processing of pro-Nedd2 directly correlated with its ability to induce cell death in transient overexpression experiments.
Keywords: 3T3 Cells
Animals
Mice
Saccharomyces cerevisiae
Enzyme Precursors
Caspases
Proteins
Recombinant Proteins
Apoptosis
Protein Processing, Post-Translational
Dimerization
Hydrolysis
Caspase 2
Rights: © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
DOI: 10.1074/jbc.273.12.6763
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