Reference: Tyers M and Futcher B (1993) Far1 and Fus3 link the mating pheromone signal transduction pathway to three G1-phase Cdc28 kinase complexes. Mol Cell Biol 13(9):5659-69

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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
Journal Article | Research Support, U.S. Gov't, P.H.S.
Authors
Tyers M, Futcher B
Primary Lit For
FAR1
Additional Lit For
CDC28 | CLN3 | FUS3 | CLN1 | CLN2 | CLN1-CDC28 kinase complex | CLN3-CDC28 kinase complex

Interaction Annotations


Genetic Interactions

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Interactor Interactor Allele Assay Annotation Action Phenotype SGA score P-value Source Reference

Physical Interactions 7 entries for 5 genes

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InteractorInteractorAssayAnnotationActionModification
CDC28FAR1Affinity Capture-Westernmanually curatedBait-HitNo Modification
CDC28FAR1Reconstituted Complexmanually curatedBait-Hitphosphorylated residue
CDC28CLN1Reconstituted Complexmanually curatedBait-HitNo Modification
CDC28CLN2Reconstituted Complexmanually curatedBait-HitNo Modification
CDC28FAR1Biochemical Activitymanually curatedBait-Hitphosphorylated residue
CLN3FAR1Affinity Capture-Westernmanually curatedBait-HitNo Modification
FAR1CLN2Reconstituted Complexmanually curatedBait-HitNo Modification
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