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Gene Review

AXL1  -  Axl1p

Saccharomyces cerevisiae S288c

Synonyms: FUS5, P9642.4, STE22, YPR122W
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Psychiatry related information on AXL1

  • Pitrilysin is a bacterial protease that is similar to the mammalian insulin-degrading enzyme, which is hypothesized to protect against the onset of Alzheimer's disease, and the yeast enzymes Axl1p and Ste23p, which are responsible for production of the a-factor mating pheromone in Saccharomyces cerevisiae [1].

High impact information on AXL1


Biological context of AXL1


Associations of AXL1 with chemical compounds

  • However, a fourth axial budding determinant, Axl1p, was absent in filamentous cells, and its abundance was controlled by glucose availability and the protein kinase Snf1p [7].

Regulatory relationships of AXL1

  • Collectively, these data indicate Ydj1p functions to promote AXL1 mRNA accumulation and in addition appears to facilitate the proper folding of nascent Axl1p [6].

Other interactions of AXL1

  • First, AXL1 mRNA levels were reduced ydj1 strains [6].
  • Consistent with an a-specific defect, the fus5 and fus8 mutants produced less a-factor than the isogenic wild-type strain [8].
  • Mutations in AXL1, STE6 and FUS3 were identified in the screen [9].
  • We also show that IDE can promote the in vivo production of the yeast a-factor mating pheromone, a function normally attributed to the yeast enzymes Axl1p and Ste23p [10].
  • First, we show that AFRP is produced intracellularly and that mutants (ste24 and axl1) that cannot produce mature a-factor due to an N-terminal processing defect are nevertheless normal for AFRP production [11].


  1. A common genetic system for functional studies of pitrilysin and related M16A proteases. Alper, B.J., Nienow, T.E., Schmidt, W.K. Biochem. J. (2006) [Pubmed]
  2. A yeast gene necessary for bud-site selection encodes a protein similar to insulin-degrading enzymes. Fujita, A., Oka, C., Arikawa, Y., Katagai, T., Tonouchi, A., Kuhara, S., Misumi, Y. Nature (1994) [Pubmed]
  3. Role of yeast insulin-degrading enzyme homologs in propheromone processing and bud site selection. Adames, N., Blundell, K., Ashby, M.N., Boone, C. Science (1995) [Pubmed]
  4. A role for a protease in morphogenic responses during yeast cell fusion. Elia, L., Marsh, L. J. Cell Biol. (1998) [Pubmed]
  5. Subcellular localization of Axl1, the cell type-specific regulator of polarity. Lord, M., Inose, F., Hiroko, T., Hata, T., Fujita, A., Chant, J. Curr. Biol. (2002) [Pubmed]
  6. Mutations in the yeast Hsp40 chaperone protein Ydj1 cause defects in Axl1 biogenesis and pro-a-factor processing. Meacham, G.C., Browne, B.L., Zhang, W., Kellermayer, R., Bedwell, D.M., Cyr, D.M. J. Biol. Chem. (1999) [Pubmed]
  7. The roles of bud-site-selection proteins during haploid invasive growth in yeast. Cullen, P.J., Sprague, G.F. Mol. Biol. Cell (2002) [Pubmed]
  8. Cell fusion during yeast mating requires high levels of a-factor mating pheromone. Brizzio, V., Gammie, A.E., Nijbroek, G., Michaelis, S., Rose, M.D. J. Cell Biol. (1996) [Pubmed]
  9. Combining mutations in the incoming and outgoing pheromone signal pathways causes a synergistic mating defect in Saccharomyces cerevisiae. Giot, L., DeMattei, C., Konopka, J.B. Yeast (1999) [Pubmed]
  10. Yeast as a tractable genetic system for functional studies of the insulin-degrading enzyme. Kim, S., Lapham, A.N., Freedman, C.G., Reed, T.L., Schmidt, W.K. J. Biol. Chem. (2005) [Pubmed]
  11. A novel a-factor-related peptide of Saccharomyces cerevisiae that exits the cell by a Ste6p-independent mechanism. Chen, P., Choi, J.D., Wang, R., Cotter, R.J., Michaelis, S. Mol. Biol. Cell (1997) [Pubmed]
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