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« Previous Abstract"Comparison of the Saccharomyces cerevisiae G1 cyclins: Cln3 may be an upstream activator of Cln1, Cln2 and other cyclins"    Next AbstractThe cyclin-dependent kinase inhibitor p40SIC1 imposes the requirement for Cln G1 cyclin function at Start »

Mol Cell Biol


Title:Far1 and Fus3 link the mating pheromone signal transduction pathway to three G1-phase Cdc28 kinase complexes
Author(s):Tyers M; Futcher B;
Address:"Banting and Best Department of Medical Research, University of Toronto, Ontario, Canada"
Journal Title:Mol Cell Biol
Year:1993
Volume:13
Issue:9
Page Number:5659 - 5669
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"

 
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