| pubmed-article:12021769 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12021769 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
| pubmed-article:12021769 | lifeskim:mentions | umls-concept:C0013138 | lld:lifeskim |
| pubmed-article:12021769 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:12021769 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:12021769 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:12021769 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:12021769 | pubmed:dateCreated | 2002-6-3 | lld:pubmed |
| pubmed-article:12021769 | pubmed:abstractText | Cell death in higher organisms is negatively regulated by Inhibitor of Apoptosis Proteins (IAPs), which contain a ubiquitin ligase motif, but how ubiquitin-mediated protein degradation is regulated during apoptosis is poorly understood. Here, we report that Drosophila melanogaster IAP1 (DIAP1) auto-ubiquitination and degradation is actively regulated by Reaper (Rpr) and UBCD1. We show that Rpr, but not Hid (head involution defective), promotes significant DIAP1 degradation. Rpr-mediated DIAP1 degradation requires an intact DIAP1 RING domain. Among the mutations affecting ubiquitination, we found ubcD1, which suppresses rpr-induced apoptosis. UBCD1 and Rpr specifically bind to DIAP1 and stimulate DIAP1 auto-ubiquitination in vitro. Our results identify a novel function of Rpr in stimulating DIAP1 auto-ubiquitination through UBCD1, thereby promoting its degradation. | lld:pubmed |
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| pubmed-article:12021769 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12021769 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12021769 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12021769 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12021769 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:12021769 | pubmed:issn | 1465-7392 | lld:pubmed |
| pubmed-article:12021769 | pubmed:author | pubmed-author:CiechanoverAa... | lld:pubmed |
| pubmed-article:12021769 | pubmed:author | pubmed-author:BergmannAndre... | lld:pubmed |
| pubmed-article:12021769 | pubmed:author | pubmed-author:StellerHerman... | lld:pubmed |
| pubmed-article:12021769 | pubmed:author | pubmed-author:RyooHyung... | lld:pubmed |
| pubmed-article:12021769 | pubmed:author | pubmed-author:GonenHedvaH | lld:pubmed |
| pubmed-article:12021769 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12021769 | pubmed:volume | 4 | lld:pubmed |
| pubmed-article:12021769 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12021769 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12021769 | pubmed:pagination | 432-8 | lld:pubmed |
| pubmed-article:12021769 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:12021769 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12021769 | pubmed:articleTitle | Regulation of Drosophila IAP1 degradation and apoptosis by reaper and ubcD1. | lld:pubmed |
| pubmed-article:12021769 | pubmed:affiliation | Howard Hughes Medical Institute, Strang Laboratory of Cancer Research, The Rockefeller University Box 252, 1230 York Ave. New York, NY 10021, USA. | lld:pubmed |
| pubmed-article:12021769 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12021769 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:12021769 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12021769 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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