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dc.contributor.authorBaliga, B.-
dc.contributor.authorColussi, P.-
dc.contributor.authorRead, S.-
dc.contributor.authorDias, M.-
dc.contributor.authorJans, D.-
dc.contributor.authorKumar, S.-
dc.identifier.citationJournal of Biological Chemistry, 2003; 278(7):4899-4905-
dc.description.abstractCaspase-2 is unique among mammalian caspases because it localizes to the nucleus in a prodomain-dependent manner. The caspase-2 prodomain also regulates caspase-2 activity via a caspase recruitment domain that mediates oligomerization of procaspase-2 molecules and their subsequent autoactivation. In this study we sought to map specific functional regions in the caspase-2 prodomain that regulate its nuclear transport and also its activation. Our data indicate that caspase-2 contains a classical nuclear localization signal (NLS) at the C terminus of the prodomain which is recognized by the importin alpha/beta heterodimer. The mutation of a conserved Lys residue in the NLS abolishes nuclear localization of caspase-2 and binding to the importin alpha/beta heterodimer. Although caspase-2 is imported into the nucleus, mutants lacking the NLS were still capable of inducing apoptosis upon overexpression in transfected cells. We define a region in the prodomain that regulates the ability of caspase-2 to form dot- and filament-like structures when ectopically expressed, which in turn promotes cell killing. Our data provides a mechanism for caspase-2 nuclear import and demonstrate that association of procaspase-2 into higher order structures, rather than its nuclear localization, is required for caspase-2 activation and its ability to induce apoptosis.-
dc.description.statementofresponsibilityBelinda C. Baliga, Paul A. Colussi, Stuart H. Read, Manisha M. Dias, David A. Jans, and Sharad Kumar-
dc.publisherAmer Soc Biochemistry Molecular Biology Inc-
dc.rights© 2002 by the American Society for Biochemistry and Molecular Biology.-
dc.subjectCOS Cells-
dc.subject3T3 Cells-
dc.subjectCell Nucleus-
dc.subjectProtein Precursors-
dc.subjectRecombinant Proteins-
dc.subjectEnzyme Activation-
dc.subjectAmino Acid Sequence-
dc.subjectProtein Structure, Tertiary-
dc.subjectProtein Transport-
dc.subjectMolecular Sequence Data-
dc.subjectCaspase 2-
dc.titleRole of prodomain in importin-mediated nuclear localization and activation of caspase-2-
dc.typeJournal article-
dc.provenancePublished online ahead of print December 10, 2002-
dc.identifier.orcidKumar, S. [0000-0001-7126-9814]-
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