Linked Life Data

10375532

Source:http://linkedlifedata.com/resource/pubmed/id/10375532

Statements in which the resource exists.
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pubmed-article:10375532pubmed:abstractTextMany tumorigenic processes affect cell-cycle progression by their effects on the levels of the cyclin-dependent kinase inhibitor p27(Kip1) [1,2]. The phosphorylation- and ubiquitination-dependent proteolysis of p27 is implicated in control of the G1-S transition in the cell cycle [3-6]. To determine the factors that control p27 stability, we established a cell-free extract assay that recapitulates the degradation of p27. Phosphorylation of p27 at Thr187 was essential for its degradation. Degradation was also dependent on SCF(Skp2), a protein complex implicated in targeting phosphorylated proteins for ubiquitination [7-10]. Immunodepletion of components of the complex - Cul-1, Skp1, or Skp2 - from the extract abolished p27 degradation, while addition of purified SCF(Skp2) to Skp2- depleted extract restored the capacity to degrade p27. A specific association was observed between Skp2 and a p27 carboxy-terminal peptide containing phosphorylated Thr187, but not between Skp2 and the non-phosphorylated peptide. Skp2-dependent associations between Skp1 or Cul-1 and the p27 phosphopeptide were also detected. Isolated SCF(Skp2) contained an E3 ubiquitin ligase activity towards p27. Our data thus suggest that SCF(Skp2) specifically targets p27 for degradation during cell-cycle progression.lld:pubmed
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pubmed-article:10375532pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:10375532pubmed:articleTitlep27(Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27.lld:pubmed
pubmed-article:10375532pubmed:affiliationDepartment of Genetics, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut 06520, USA.lld:pubmed
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pubmed-article:10375532pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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