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.
Dates
Type | When |
---|---|
Created | 9 years, 10 months ago (Oct. 5, 2015, 8:36 p.m.) |
Deposited | 2 years, 8 months ago (Dec. 15, 2022, 9:09 a.m.) |
Indexed | 1 year, 1 month ago (July 10, 2024, 11:21 a.m.) |
Issued | 31 years, 11 months ago (Sept. 1, 1993) |
Published | 31 years, 11 months ago (Sept. 1, 1993) |
Published Online | 31 years, 11 months ago (Sept. 1, 1993) |
Published Print | 31 years, 11 months ago (Sept. 1, 1993) |
@article{Tyers_1993, title={Far1 and Fus3 link the mating pheromone signal transduction pathway to three G1-phase Cdc28 kinase complexes.}, volume={13}, ISSN={1098-5549}, url={http://dx.doi.org/10.1128/mcb.13.9.5659}, DOI={10.1128/mcb.13.9.5659}, number={9}, journal={Molecular and Cellular Biology}, publisher={Informa UK Limited}, author={Tyers, M and Futcher, B}, year={1993}, month=sep, pages={5659–5669} }