Tyers, M., Futcher, B. (March 1994) Far1 and Fus3 Link the Mating Pheromone Signal-Transduction Pathway to 3 G(1)-Phase Cdc28 Kinase Complexes. Molecular and Cellular Biology, 14 (3). p. 2222. ISSN 0270-7306
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 |
|---|---|
| Subjects: | 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 organs, tissues, organelles, cell types and functions > tissues types and functions > signal transduction |
| CSHL Authors: | |
| Communities: | CSHL labs > Futcher lab |
| Depositing User: | Matt Covey |
| Date: | March 1994 |
| Date Deposited: | 04 May 2015 19:55 |
| Last Modified: | 04 May 2015 19:55 |
| PMCID: | PMC360296 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/31485 |
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