The Cln3-Cdc28 kinase complex of S. cerevisiae is regulated by proteolysis and phosphorylation

Tyers, M., Tokiwa, G., Nash, R., Futcher, B. (May 1992) The Cln3-Cdc28 kinase complex of S. cerevisiae is regulated by proteolysis and phosphorylation. Embo Journal, 11 (5). pp. 1773-1784. ISSN 0261-4189

URL: http://www.ncbi.nlm.nih.gov/pubmed/1316273

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.

Item Type: Paper
Uncontrolled Keywords: CELL CYCLE CDC34 G1 CYCLIN PEST HYPOTHESIS START YEAST-CELL CYCLE P34CDC2 PROTEIN-KINASE SACCHAROMYCES-CEREVISIAE FISSION YEAST MATING-PHEROMONE DIVISION CYCLE M-PHASE GENE ARREST CDC2
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression > phosphorylation
organism description > yeast
CSHL Authors:
Communities: CSHL labs > Futcher lab
Depositing User: Matt Covey
Date: May 1992
Date Deposited: 01 Oct 2015 15:18
Last Modified: 01 Oct 2015 15:18
PMCID: PMC556635
URI: http://repository.cshl.edu/id/eprint/31790

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