| pubmed-article:11032804 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11032804 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:11032804 | lifeskim:mentions | umls-concept:C0016030 | lld:lifeskim |
| pubmed-article:11032804 | lifeskim:mentions | umls-concept:C1167313 | lld:lifeskim |
| pubmed-article:11032804 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:11032804 | lifeskim:mentions | umls-concept:C0381943 | lld:lifeskim |
| pubmed-article:11032804 | lifeskim:mentions | umls-concept:C1335831 | lld:lifeskim |
| pubmed-article:11032804 | lifeskim:mentions | umls-concept:C1519751 | lld:lifeskim |
| pubmed-article:11032804 | lifeskim:mentions | umls-concept:C1332809 | lld:lifeskim |
| pubmed-article:11032804 | lifeskim:mentions | umls-concept:C0444669 | lld:lifeskim |
| pubmed-article:11032804 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:11032804 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:11032804 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:11032804 | lifeskim:mentions | umls-concept:C0301625 | lld:lifeskim |
| pubmed-article:11032804 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:11032804 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:11032804 | pubmed:dateCreated | 2000-11-28 | lld:pubmed |
| pubmed-article:11032804 | pubmed:abstractText | The ubiquitin protein ligase SCF(Skp2) is composed of Skp1, Cul1, Roc1/Rbx1 and the F-box protein Skp2, the substrate-recognition subunit. Levels of Skp2 decrease as cells exit the cell cycle and increase as cells re-enter the cycle. Ectopic expression of Skp2 in quiescent fibroblasts causes mitogen-independent S-phase entry. Hence, mechanisms must exist for limiting Skp2 protein expression during the G(0)/G(1) phases. Here we show that Skp2 is degraded by the proteasome in G(0)/G(1) and is stabilized when cells re-enter the cell cycle. Rapid degradation of Skp2 in quiescent cells depends on Skp2 sequences that contribute to Cul1 binding and interference with endogenous Cul1 function in serum-deprived cells induces Skp2 expression. Furthermore, recombinant Cul1-Roc1/Rbx1-Skp1 complexes can catalyse Skp2 ubiquitylation in vitro. These results suggest that degradation of Skp2 in G(0)/G(1) is mediated, at least in part, by an autocatalytic mechanism involving a Skp2-bound Cul1-based core ubiquitin ligase and imply a role for this mechanism in the suppression of SCF(Skp2) ubiquitin protein ligase function during the G(0)/G(1) phases of the cell cycle. | lld:pubmed |
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| pubmed-article:11032804 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11032804 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11032804 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11032804 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11032804 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11032804 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11032804 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11032804 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11032804 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11032804 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11032804 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11032804 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11032804 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11032804 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:11032804 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:11032804 | pubmed:author | pubmed-author:PeterMM | lld:pubmed |
| pubmed-article:11032804 | pubmed:author | pubmed-author:ReymondFF | lld:pubmed |
| pubmed-article:11032804 | pubmed:author | pubmed-author:KreyAA | lld:pubmed |
| pubmed-article:11032804 | pubmed:author | pubmed-author:BlondelMM | lld:pubmed |
| pubmed-article:11032804 | pubmed:author | pubmed-author:WirbelauerCC | lld:pubmed |
| pubmed-article:11032804 | pubmed:author | pubmed-author:GstaigerMM | lld:pubmed |
| pubmed-article:11032804 | pubmed:author | pubmed-author:SutterlütyHH | lld:pubmed |
| pubmed-article:11032804 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11032804 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:11032804 | pubmed:volume | 19 | lld:pubmed |
| pubmed-article:11032804 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11032804 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11032804 | pubmed:pagination | 5362-75 | lld:pubmed |
| pubmed-article:11032804 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:11032804 | pubmed:meshHeading | pubmed-meshheading:11032804... | lld:pubmed |
| pubmed-article:11032804 | pubmed:meshHeading | pubmed-meshheading:11032804... | lld:pubmed |
| pubmed-article:11032804 | pubmed:meshHeading | pubmed-meshheading:11032804... | lld:pubmed |
| pubmed-article:11032804 | pubmed:meshHeading | pubmed-meshheading:11032804... | lld:pubmed |
| pubmed-article:11032804 | pubmed:meshHeading | pubmed-meshheading:11032804... | lld:pubmed |
