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- W172411893 abstract "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." @default.
- W172411893 created "2016-06-24" @default.
- W172411893 creator A5057700057 @default.
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- W172411893 date "1992-05-01" @default.
- W172411893 modified "2023-10-11" @default.
- W172411893 title "The Cln3-Cdc28 kinase complex of S. cerevisiae is regulated by proteolysis and phosphorylation." @default.
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- W172411893 doi "https://doi.org/10.1002/j.1460-2075.1992.tb05229.x" @default.
- W172411893 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/556635" @default.
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