Far1 and Fus3 Link the Mating Pheromone Signal-Transduction Pathway to 3 G1-Phase Cdc28 Kinase Complexes

Tyers, M., Futcher, B. (1993) Far1 and Fus3 Link the Mating Pheromone Signal-Transduction Pathway to 3 G1-Phase Cdc28 Kinase Complexes. Mol Cell Biol, 13 (9). pp. 5659-5669. ISSN 0270-7306

URL: http://www.ncbi.nlm.nih.gov/pubmed/8395009
DOI: 10.1128/MCB.13.9.5659

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.

Item Type: Paper
Uncontrolled Keywords: CELL-CYCLE CONTROL SACCHAROMYCES-CEREVISIAE PROTEIN-KINASE RESPONSE PATHWAY YEAST GENE ARREST DIVISION CLN2 PHOSPHORYLATION
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > Cyclins
organs, tissues, organelles, cell types and functions > cell types and functions > cell functions > cell cycle
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 Deposited: 13 Apr 2016 19:18
Last Modified: 13 Apr 2016 19:18
PMCID: PMC360296
Related URLs:
URI: http://repository.cshl.edu/id/eprint/32564

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