| pubmed-article:12477715 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12477715 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:12477715 | lifeskim:mentions | umls-concept:C0521447 | lld:lifeskim |
| pubmed-article:12477715 | lifeskim:mentions | umls-concept:C0259419 | lld:lifeskim |
| pubmed-article:12477715 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:12477715 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:12477715 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:12477715 | pubmed:dateCreated | 2003-2-10 | lld:pubmed |
| pubmed-article:12477715 | pubmed:abstractText | Caspase-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. | lld:pubmed |
| pubmed-article:12477715 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12477715 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12477715 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12477715 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12477715 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12477715 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12477715 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12477715 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:12477715 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:12477715 | pubmed:author | pubmed-author:KumarSharadS | lld:pubmed |
| pubmed-article:12477715 | pubmed:author | pubmed-author:JansDavid ADA | lld:pubmed |
| pubmed-article:12477715 | pubmed:author | pubmed-author:BaligaBelinda... | lld:pubmed |
| pubmed-article:12477715 | pubmed:author | pubmed-author:ReadStuart... | lld:pubmed |
| pubmed-article:12477715 | pubmed:author | pubmed-author:ColussiPaul... | lld:pubmed |
| pubmed-article:12477715 | pubmed:author | pubmed-author:DiasManisha... | lld:pubmed |
| pubmed-article:12477715 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12477715 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:12477715 | pubmed:volume | 278 | lld:pubmed |
| pubmed-article:12477715 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12477715 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12477715 | pubmed:pagination | 4899-905 | lld:pubmed |
| pubmed-article:12477715 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:12477715 | pubmed:meshHeading | pubmed-meshheading:12477715... | lld:pubmed |
| pubmed-article:12477715 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12477715 | pubmed:articleTitle | Role of prodomain in importin-mediated nuclear localization and activation of caspase-2. | lld:pubmed |
| pubmed-article:12477715 | pubmed:affiliation | Hanson Institute, Frome Road, Adelaide 5000, Australia. | lld:pubmed |
| pubmed-article:12477715 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12477715 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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