Reference: Tyers M and Futcher B (1993)
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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.
- Reference Type
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Journal Article |
Research Support, U.S. Gov't, P.H.S.
- Authors
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Tyers M,
Futcher B
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- FAR1
- CDC28 | CLN3 | FUS3 | CLN1 | CLN2 | CLN1-CDC28 kinase complex | CLN3-CDC28 kinase complex
Gene Ontology Annotations
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Regulator Systematic Name |
Target |
Target Systematic Name |
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Post-translational Modifications
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| Interactor | Interactor | Assay | Annotation | Action | Modification |
| CDC28 | FAR1 | Affinity Capture-Western | manually curated | Bait-Hit | No Modification |
| CDC28 | FAR1 | Reconstituted Complex | manually curated | Bait-Hit | phosphorylated residue |
| CDC28 | CLN1 | Reconstituted Complex | manually curated | Bait-Hit | No Modification |
| CDC28 | CLN2 | Reconstituted Complex | manually curated | Bait-Hit | No Modification |
| CDC28 | FAR1 | Biochemical Activity | manually curated | Bait-Hit | phosphorylated residue |
| CLN3 | FAR1 | Affinity Capture-Western | manually curated | Bait-Hit | No Modification |
| FAR1 | CLN2 | Reconstituted Complex | manually curated | Bait-Hit | No Modification |
Functional Complementation Annotations
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Complement ID |
Locus ID |
Gene |
Species |
Gene ID |
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Direction |
Details |
Source |
Reference |