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PMID: 8395009 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Far1 and Fus3 link the mating pheromone signal transduction pathway to three G1-phase Cdc28 kinase complexes.

Molecular and cellular biology ·Vol. 13 ·No. 9 ·1993-09-00 ·Pages 5659-69

Tyers M, Futcher B

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.

Related Genes
MeSH Terms
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 Macromolecular Substances Mating Factor Mitogen-Activated Protein Kinases Molecular Sequence Data Peptides/metabolism Phosphoproteins/metabolism Phosphorylation Protein Binding Protein Kinases/metabolism Repressor Proteins Saccharomyces cerevisiae/cytology Saccharomyces cerevisiae Proteins Signal Transduction
Chemicals
CLN1 protein, S cerevisiae CLN2 protein, S cerevisiae CLN3 protein, S cerevisiae Cell Cycle Proteins Cyclin-Dependent Kinase Inhibitor Proteins Cyclins FAR1 protein, S cerevisiae Fungal Proteins Macromolecular Substances Peptides Phosphoproteins Repressor Proteins Saccharomyces cerevisiae Proteins Mating Factor Protein Kinases Calcium-Calmodulin-Dependent Protein Kinases CDC28 Protein Kinase, S cerevisiae FUS3 protein, S cerevisiae Mitogen-Activated Protein Kinases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Tyers M
Banting and Best Department of Medical Research, University of Toronto, Ontario, Canada.
Futcher B
References (33)
33 references, click to expand
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
Published
1993-09-00
Pages
5659-69
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC360296
Subset
IM
Grants
NIGMS NIH HHS · GM39978 · United States
Corrections
ErratumIn
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