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CDC42 — FAR1

Text-mined interactions from Literome

Nern et al., J Cell Biol 1999 : Here we show that a two- hybrid interaction between Cdc24p and Gbeta requires Far1p but not pheromone dependent MAP-kinase signaling, indicating Far1p has a role in regulating the association of Cdc24p and Gbeta
Nern et al., J Cell Biol 2000 : Far1p is necessary and sufficient for nuclear accumulation of Cdc24p , suggesting that its nuclear import occurs via an association with Far1p
Blondel et al., EMBO J 2000 : Nuclear-specific degradation of Far1 is controlled by the localization of the F-box protein Cdc4 ... A cytoplasmic form of Cdc4 was unable to complement the growth defect of cdc4-1 cells, but it was sufficient to degrade Far1 in the cytoplasm
Wiget et al., EMBO J 2004 : Site-specific regulation of the GEF Cdc24p by the scaffold protein Far1p during yeast mating ... Here we investigated the role of Far1p in the regulation of Cdc24p in vivo ... Using time-lapse microscopy of mating cells and artificial membrane targeting of Far1p, we show that Far1p is necessary and sufficient to recruit Cdc24p to the plasma membrane
Peter et al., Science 1994 : The kinase activity of Cdc28-Cln was directly inhibited by Far1 both in vivo and in vitro, thus demonstrating that Far1 acts at the final step in the alpha-factor response pathway by inhibiting a G1 cyclin dependent kinase
Peter et al., Cell 1993 : We show also that FAR1 is phosphorylated in vitro by the CDC28-CLN2 complex and in vivo in a CDC28 dependent manner
Horecka et al., Genetics 1996 : As a first step toward elucidating the mechanism by which Far3 promotes pheromone mediated G1 arrest, we performed genetic and molecular experiments to test the possibility that Far3 participates in one of the heretofore characterized mechanisms, namely Fus3/Far1 mediated inhibition of Cdc28-Cln kinase activity, G1 cyclin gene repression, and G1 cyclin protein turnover