Alpha factor induces arrest of yeast a cells in G1 and transcription of genes involved in mating. Prior work indicates that FUS3, a member of the MAP kinase family, and FAR1, whose molecular activity is unknown, contribute to cell cycle arrest by inhibiting G1 cyclins. Here we show that FAR1 is a substrate for FUS3 and that this phosphorylation regulates association of FAR1 with CDC28-CLN2 kinase. We show also that FAR1 is phosphorylated in vitro by the CDC28-CLN2 complex and in vivo in a CDC28-dependent manner. Mutational analysis of FAR1 reveals a correlation between its ability to associate with CDC28-CLN2 and to arrest the cell cycle. These results suggest that FAR1 protein is the link between the signaling pathway and the cell cycle machinery.