Prodomain-dependent neclear localisation of the caspase-2 (Nedd2) precursor: A novel fuction for a caspase prodomain
Date
1998
Authors
Colussi, P.
Harvey, N.
Kumar, S.
Editors
Advisors
Journal Title
Journal ISSN
Volume Title
Type:
Journal article
Citation
Journal of Biological Chemistry, 1998; 273(38):24535-24542
Statement of Responsibility
Paul A. Colussi, Natasha L. Harvey and Sharad Kumar
Conference Name
Abstract
Caspases are cysteine proteases that play an essential role in apoptosis by cleaving several key cellular proteins. Despite their function in apoptosis, little is known about where in the cell they are localized and whether they are translocated to specific cellular compartments upon activation. In the present paper, usingAequorea victoria green fluorescent protein fusion constructs, we have determined the localization of Nedd2 (mouse caspase-2) and show that both precursor and processed caspase-2 localize to the cytoplasmic and the nuclear compartments. We demonstrate that the nuclear localization of caspase-2 is strictly dependent on the presence of the prodomain. A caspase-2 prodomain-green fluorescent protein localized to dot- and fiber-like structures mostly in the nucleus, whereas a protein lacking the prodomain was largely concentrated in the cytoplasm. We also show that an amino-terminal fusion of the prodomain of caspase-2 to caspase-3 mediates nuclear transport of caspase-3, which is normally localized in the cytoplasm. These results suggest that, in addition to roles in dimerization and recruitment through adaptors, the caspase-2 prodomain has a novel function in nuclear transport.
School/Discipline
Dissertation Note
Provenance
Description
Access Status
Rights
© 1998 by The American Society for Biochemistry and Molecular Biology, Inc.