Title: | Far1 and Fus3 link the mating pheromone signal transduction pathway to three G1-phase Cdc28 kinase complexes |
Address: | "Banting and Best Department of Medical Research, University of Toronto, Ontario, Canada" |
DOI: | 10.1128/mcb.13.9.5659-5669.1993 |
ISSN/ISBN: | 0270-7306 (Print) 1098-5549 (Electronic) 0270-7306 (Linking) |
Abstract: | "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" |
Keywords: | "Amino Acid Sequence CDC28 Protein Kinase, S cerevisiae/*metabolism Calcium-Calmodulin-Dependent Protein Kinases *Cell Cycle *Cell Cycle Proteins Cyclin-Dependent Kinase Inhibitor Proteins Cyclins/metabolism Fungal Proteins/*metabolism Kinetics Macromolecu;" |
Notes: | "MedlineTyers, M Futcher, B eng GM39978/GM/NIGMS NIH HHS/ Research Support, U.S. Gov't, P.H.S. 1993/09/01 Mol Cell Biol. 1993 Sep; 13(9):5659-69. doi: 10.1128/mcb.13.9.5659-5669.1993" |