| pubmed-article:1316273 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1316273 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
| pubmed-article:1316273 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:1316273 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:1316273 | lifeskim:mentions | umls-concept:C0597304 | lld:lifeskim |
| pubmed-article:1316273 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:1316273 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:1316273 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:1316273 | pubmed:dateCreated | 1992-6-16 | lld:pubmed |
| pubmed-article:1316273 | pubmed:abstractText | In Saccharomyces cerevisiae, several of the proteins involved in the Start decision have been identified; these include the Cdc28 protein kinase and three cyclin-like proteins, Cln1, Cln2 and Cln3. We find that Cln3 is a very unstable, low abundance protein. In contrast, the truncated Cln3-1 protein is stable, suggesting that the PEST-rich C-terminal third of Cln3 is necessary for rapid turnover. Cln3 associates with Cdc28 to form an active kinase complex that phosphorylates Cln3 itself and a co-precipitated substrate of 45 kDa. The cdc34-2 allele, which encodes a defective ubiquitin conjugating enzyme, dramatically increases the kinase activity associated with Cln3, but does not affect the half-life of Cln3. The Cln--Cdc28 complex is inactivated by treatment with non-specific phosphatases; prolonged incubation with ATP restores kinase activity to the dephosphorylated kinase complex. It is thus possible that phosphate residues essential for Cln-Cdc28 kinase activity are added autocatalytically. The multiple post-translational controls on Cln3 activity may help Cln3 tether division to growth. | lld:pubmed |
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| pubmed-article:1316273 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1316273 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1316273 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1316273 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1316273 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1316273 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1316273 | pubmed:month | May | lld:pubmed |
| pubmed-article:1316273 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:1316273 | pubmed:author | pubmed-author:NashRR | lld:pubmed |
| pubmed-article:1316273 | pubmed:author | pubmed-author:FutcherBB | lld:pubmed |
| pubmed-article:1316273 | pubmed:author | pubmed-author:TyersMM | lld:pubmed |
| pubmed-article:1316273 | pubmed:author | pubmed-author:TokiwaGG | lld:pubmed |
| pubmed-article:1316273 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1316273 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:1316273 | pubmed:geneSymbol | CLN3 | lld:pubmed |
| pubmed-article:1316273 | pubmed:geneSymbol | CLN1 | lld:pubmed |
| pubmed-article:1316273 | pubmed:geneSymbol | CLN2 | lld:pubmed |
| pubmed-article:1316273 | pubmed:geneSymbol | CDC34 | lld:pubmed |
| pubmed-article:1316273 | pubmed:geneSymbol | cdc34-2 | lld:pubmed |
| pubmed-article:1316273 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1316273 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1316273 | pubmed:pagination | 1773-84 | lld:pubmed |
| pubmed-article:1316273 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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| pubmed-article:1316273 | pubmed:meshHeading | pubmed-meshheading:1316273-... | lld:pubmed |
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| pubmed-article:1316273 | pubmed:meshHeading | pubmed-meshheading:1316273-... | lld:pubmed |
