Far1 and Fus3 link the mating pheromone signal transduction pathway to three G1-phase Cdc28 kinase complexes.

In the yeast Saccharomyces cerevisiae, the Cdc28 protein kinase controls commitment to cell division at Start, but no biologically relevant G1-phase substrates have been identified. We have studied the kinase complexes formed between Cdc28 and each of the G1 cyclins Cln1, Cln2, and Cln3. Each complex has a specific array ...
of coprecipitated in vitro substrates. We identify one of these as Far1, a protein required for pheromone-induced arrest at Start. Treatment with alpha-factor induces a preferential association and/or phosphorylation of Far1 by the Cln1, Cln2, and Cln3 kinase complexes. This induced interaction depends upon the Fus3 protein kinase, a mitogen-activated protein kinase homolog that functions near the bottom of the alpha-factor signal transduction pathway. Thus, we trace a path through which a mitogen-activated protein kinase regulates a Cdc2 kinase.
Mesh Terms:
Amino Acid Sequence, CDC28 Protein Kinase, S cerevisiae, Calcium-Calmodulin-Dependent Protein Kinases, Cell Cycle, Cell Cycle Proteins, Cyclin-Dependent Kinase Inhibitor Proteins, Cyclins, Fungal Proteins, Kinetics, Macromolecular Substances, Mitogen-Activated Protein Kinases, Molecular Sequence Data, Peptides, Phosphoproteins, Phosphorylation, Protein Binding, Protein Kinases, Repressor Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Signal Transduction
Mol. Cell. Biol.
Date: Sep. 01, 1993
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