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Gene Review

FAR1  -  Far1p

Saccharomyces cerevisiae S288c

Synonyms: CKI FAR1, Cyclin-dependent kinase inhibitor FAR1, Factor arrest protein, J0565, YJL157C
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Disease relevance of FAR1

  • Interestingly, expression of membrane-targeted Far1p causes toxicity, most likely by activating Cdc42p uniformly at the cell cortex [1].

High impact information on FAR1


Biological context of FAR1


Anatomical context of FAR1

  • Thus, Far1p functions as an adaptor that recruits polarity establishment proteins to the site of extracellular signaling marked by Gbetagamma to polarize assembly of the cytoskeleton in a morphogenetic gradient [7].
  • Here we show that SCF(Cdc4) ubiquitylates Far1 in the nucleus, which in turn targets the multi-ubiquitylated protein to 26S proteasomes most likely located at the nuclear envelope [8].
  • 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 [1].

Associations of FAR1 with chemical compounds

  • Cln3 Delta, far1 Delta, and strains overexpressing Far1 do not delay budding during an ethanol glucose shift-up as wild type does [6].
  • In contrast, threonine 306 seems to be an important recipient of an activating modification, as substitutions at this position abolish the G1 arrest function of Far1 [9].
  • A change of serine 87 to alanine prevents the cell cycle-dependent degradation of Far1, causing enhanced sensitivity to pheromone [9].

Physical interactions of FAR1

  • In response to mating pheromones, a fraction of Far1 was stabilized after its export into the cytoplasm by Ste21/Msn5 [8].
  • Strikingly, Bem1 also copurifies with Far1, a Fus3 substrate required for G1 arrest and proper polarized growth during mating [10].

Regulatory relationships of FAR1

  • The pattern of cell cycle-regulated transcription of FAR1 could involve combinatorial control of Ste12 and Mcm1 [11].
  • Fus3p is known to promote G1 arrest by activating Far1p, which inhibits three Clnp/Cdc28p kinases [12].
  • Ste12 and Mcm1 regulate cell cycle-dependent transcription of FAR1 [11].
  • Together, these findings indicate that Cln3 has to overcome Far1 to trigger Cln-Cdc28 activation, which then turns on SBF- and MBF-dependent transcription [6].
  • Our results imply that Gbetagamma not only targets Far1p to the correct site but may also trigger a conformational change in Far1p that is required for its ability to activate Cdc24p in vivo [1].

Other interactions of FAR1

  • Identification of a gene necessary for cell cycle arrest by a negative growth factor of yeast: FAR1 is an inhibitor of a G1 cyclin, CLN2 [3].
  • CLN1 overexpression had a similar effect when the FAR1 gene, encoding a negative regulator of CLN1/2 function, was deleted [13].
  • The cell cycle transcription pattern for FAR1 was changed in ste12- cells: the gene was still significantly expressed in G2/M, but transcript levels were strongly reduced in G1 phase, resulting in a lack of Far1 protein accumulation [11].
  • We conclude that the FAR3-dependent arrest pathway is functionally distinct from that which employs FAR1 [14].
  • We find that Fus3p and Kss1p both control G1 arrest through multiple functions that operate in parallel with Far1p [12].


  1. Site-specific regulation of the GEF Cdc24p by the scaffold protein Far1p during yeast mating. Wiget, P., Shimada, Y., Butty, A.C., Bi, E., Peter, M. EMBO J. (2004) [Pubmed]
  2. FAR1 links the signal transduction pathway to the cell cycle machinery in yeast. Peter, M., Gartner, A., Horecka, J., Ammerer, G., Herskowitz, I. Cell (1993) [Pubmed]
  3. Identification of a gene necessary for cell cycle arrest by a negative growth factor of yeast: FAR1 is an inhibitor of a G1 cyclin, CLN2. Chang, F., Herskowitz, I. Cell (1990) [Pubmed]
  4. FAR1 is required for posttranscriptional regulation of CLN2 gene expression in response to mating pheromone. Valdivieso, M.H., Sugimoto, K., Jahng, K.Y., Fernandes, P.M., Wittenberg, C. Mol. Cell. Biol. (1993) [Pubmed]
  5. Phosphorylation- and ubiquitin-dependent degradation of the cyclin-dependent kinase inhibitor Far1p in budding yeast. Henchoz, S., Chi, Y., Catarin, B., Herskowitz, I., Deshaies, R.J., Peter, M. Genes Dev. (1997) [Pubmed]
  6. A cell sizer network involving Cln3 and Far1 controls entrance into S phase in the mitotic cycle of budding yeast. Alberghina, L., Rossi, R.L., Querin, L., Wanke, V., Vanoni, M. J. Cell Biol. (2004) [Pubmed]
  7. The role of Far1p in linking the heterotrimeric G protein to polarity establishment proteins during yeast mating. Butty, A.C., Pryciak, P.M., Huang, L.S., Herskowitz, I., Peter, M. Science (1998) [Pubmed]
  8. Nuclear-specific degradation of Far1 is controlled by the localization of the F-box protein Cdc4. Blondel, M., Galan, J.M., Chi, Y., Lafourcade, C., Longaretti, C., Deshaies, R.J., Peter, M. EMBO J. (2000) [Pubmed]
  9. Pheromone-dependent G1 cell cycle arrest requires Far1 phosphorylation, but may not involve inhibition of Cdc28-Cln2 kinase, in vivo. Gartner, A., Jovanović, A., Jeoung, D.I., Bourlat, S., Cross, F.R., Ammerer, G. Mol. Cell. Biol. (1998) [Pubmed]
  10. The SH3-domain protein Bem1 coordinates mitogen-activated protein kinase cascade activation with cell cycle control in Saccharomyces cerevisiae. Lyons, D.M., Mahanty, S.K., Choi, K.Y., Manandhar, M., Elion, E.A. Mol. Cell. Biol. (1996) [Pubmed]
  11. Ste12 and Mcm1 regulate cell cycle-dependent transcription of FAR1. Oehlen, L.J., McKinney, J.D., Cross, F.R. Mol. Cell. Biol. (1996) [Pubmed]
  12. Fus3p and Kss1p control G1 arrest in Saccharomyces cerevisiae through a balance of distinct arrest and proliferative functions that operate in parallel with Far1p. Cherkasova, V., Lyons, D.M., Elion, E.A. Genetics (1999) [Pubmed]
  13. G1 cyclins CLN1 and CLN2 repress the mating factor response pathway at Start in the yeast cell cycle. Oehlen, L.J., Cross, F.R. Genes Dev. (1994) [Pubmed]
  14. Far3 and five interacting proteins prevent premature recovery from pheromone arrest in the budding yeast Saccharomyces cerevisiae. Kemp, H.A., Sprague, G.F. Mol. Cell. Biol. (2003) [Pubmed]
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