| pubmed-article:10733526 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10733526 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:10733526 | lifeskim:mentions | umls-concept:C0162832 | lld:lifeskim |
| pubmed-article:10733526 | lifeskim:mentions | umls-concept:C0694872 | lld:lifeskim |
| pubmed-article:10733526 | lifeskim:mentions | umls-concept:C1826553 | lld:lifeskim |
| pubmed-article:10733526 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:10733526 | lifeskim:mentions | umls-concept:C0599894 | lld:lifeskim |
| pubmed-article:10733526 | lifeskim:mentions | umls-concept:C0179400 | lld:lifeskim |
| pubmed-article:10733526 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:10733526 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:10733526 | pubmed:dateCreated | 2000-5-1 | lld:pubmed |
| pubmed-article:10733526 | pubmed:abstractText | The ordered progression through the cell cycle depends on regulating the abundance of several proteins through ubiquitin-mediated proteolysis. Degradation is precisely timed and specific. One key component of the degradation system, the anaphase promoting complex (APC), is a ubiquitin protein ligase. It is activated both during mitosis and late in mitosis/G(1), by the WD repeat proteins Cdc20 and Cdh1, respectively. These activators target distinct sets of substrates. Cdc20-APC requires a well-defined destruction box (D box), whereas Cdh1-APC confers a different and as yet unidentified specificity. We have determined the sequence specificity for Cdh1-APC using two assays, ubiquitination in a completely defined and purified system and degradation promoted by Cdh1-APC in Xenopus extracts. Cdc20 is itself a Cdh1-APC substrate. Vertebrate Cdc20 lacks a D box and therefore is recognized by Cdh1-APC through a different sequence. By analysis of Cdc20 as a substrate, we have identified a new recognition signal. This signal, composed of K-E-N, serves as a general targeting signal for Cdh1-APC. Like the D box, it is transposable to other proteins. Using the KEN box as a template, we have identified cell cycle genes Nek2 and B99 as additional Cdh1-APC substrates. Mutation in the KEN box stabilizes all three proteins against ubiquitination and degradation. | lld:pubmed |
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| pubmed-article:10733526 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10733526 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10733526 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10733526 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:10733526 | pubmed:issn | 0890-9369 | lld:pubmed |
| pubmed-article:10733526 | pubmed:author | pubmed-author:KirschnerM... | lld:pubmed |
| pubmed-article:10733526 | pubmed:author | pubmed-author:PflegerC MCM | lld:pubmed |
| pubmed-article:10733526 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10733526 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:10733526 | pubmed:volume | 14 | lld:pubmed |
| pubmed-article:10733526 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10733526 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10733526 | pubmed:pagination | 655-65 | lld:pubmed |
| pubmed-article:10733526 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:10733526 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10733526 | pubmed:articleTitle | The KEN box: an APC recognition signal distinct from the D box targeted by Cdh1. | lld:pubmed |
| pubmed-article:10733526 | pubmed:affiliation | Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115 USA. | lld:pubmed |
| pubmed-article:10733526 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10733526 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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